Structure and Function of Proteins

Structural biologists aim at deriving an understanding of the molecular basis of biological phenomena by obtaining images of the involved biomacromolecules at atomic resolution. We use protein crystallography to investigate proteins that play a role in infectious disease, e.g. by controlling the production of toxic molecules or by acting as toxins themselves. Our research in structural biology is complemented by biochemical and biophysical methods, and we also employ all these technologies to aid drug discovery projects at the HZI. 


Selected Publications

Witzgall F, Erwert W, Blankenfeldt W (2017). Structures of the N-terminal domain of PqsA in complex with anthraniloyl- and 6-fluoroanthraniloyl-AMP: substrate activation in Pseudomonas Quinolone Signal (PQS) biosynthesis. Chembiochem 18:2045-55.

Diederich C#, Leypold M#, Culka M#, Weber HJ, Breinbauer R*, Ullmann GM* & Blankenfeldt W* (2017). Mechanisms and specificity of phenazine biosynthesis protein PhzF. Sci Rep. 7:6272. #equal contribution; *corresponding authors

Bock T, Luxenburger E, Hoffmann J, Schütza V, Feiler C, Müller R & Blankenfeldt W (2017). AibA/AibB induces an intramolecular decarboxylation in de novo isovalerate biosynthesis of Myxococcus xanthus. Angew Chem Int Ed Engl. 56:9986-9

Bock T, Volz C, Hering V, Scrima A, Müller R, Blankenfeldt W (2017). The AibR-isovaleryl coenzyme A regulator and its DNA binding site - a model for the regulation of alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus. Nucleic Acids Res. 45:2166-78.

Zender M, Witzgall F, Drees SL, Weidel E, Maurer CK, Fetzner S, Blankenfeldt W, Empting M* & Hartmann RW* (2016). Dissecting the Multiple Roles of PqsE in Pseudomonas aeruginosa Virulence by Discovery of Small Tool Compounds. ACS Chem Biol 11:1755-63; * corresponding authors


A. Research Papers

83.    Friedel K, Popp MA, Matern JCJ, Gazdag EM, Thiel IV, Volkmann G, Blankenfeldt W, Mootz HD. (2018). A functional interplay between intein and extein sequences in protein splicing compensates for the essential block B histidine. Chem Sci. 10:239-51.

82.    Schaks M, Singh SP, Kage F, Thomason P, Klünemann T, Steffen A, Blankenfeldt W, Stradal TE, Insall RH, Rottner K (2018). Distinct Interaction Sites of Rac GTPase with WAVE Regulatory Complex Have Non-redundant Functions in Vivo. Curr Biol. 28:3674-84.

81.    Sung KH, Josewski J, Dübel S, Blankenfeldt W, Rau U (2018). Structural insights into  antigen recognition of an anti-β-(1,6)-β-(1,3)-D-glucan antibody. Sci Rep. 8:13652.

80.    Fiebig D, Storka J, Roeder M, Meyners C, Schmelz S, Blankenfeldt W, Scrima A,  Kolmar H, Fuchsbauer HL (2018). Destructive twisting of neutral metalloproteases: the catalysis mechanism of the Dispase autolysis-inducing protein from Streptomyces mobaraensis DSM 40487. FEBS J. 285:4246-64.

79.    Schwemmlein N#, Pippel J#, Gazdag EM, Blankenfeldt W (2018). Crystal Structures of R-Type Bacteriocin Sheath and Tube Proteins CD1363 and CD1364 From Clostridium difficile in the Pre-assembled State. Front Microbiol. 9:1750. #equal contribution

78.    Poppe J, Reichelt J, Blankenfeldt W. (2018). Pseudomonas aeruginosa pyoverdine maturation enzyme PvdP has a noncanonical domain architecture and affords insight into a new subclass of tyrosinases. J Biol Chem. 293:14926-36.

77.    Witzgall F, Depke T, Hoffmann M, Empting M, Brönstrup M, Müller R, Blankenfeldt W (2018). The Alkylquinolone Repertoire of Pseudomonas aeruginosa is linked to Structural Flexibility of the FabH-like PQS Biosynthesis Enzyme PqsBC. Chembiochem 19:1531-44.

76.    Krausze J, Hercher TW, Zwerschke D, Kirk ML, Blankenfeldt W, Mendel RR, Kruse T (2018). The functional principle of eukaryotic molybdenum insertases. Biochem J. 475:1739-53.

75.    Misson L, Burn R, Vit A, Hildesheim J, Beliaeva MA, Blankenfeldt W, Seebeck FP (2018). Inhibition and Regulation of the Ergothioneine Biosynthetic Methyltransferase EgtD. ACS Chem Biol. 13:1333-42.

74.    Sung KH, Berkhan G, Hollmann T, Wagner L, Blankenfeldt W, Hahn F (2018). Insights into the dual Activity of a Bifunctional Dehydratase-Cyclase Domain. Angew Chem Int Ed Engl. 57:343-7

73.    Koopmeiers J, Diederich C, Solarczek J, Voss H, Mayer J, Blankenfeldt W, Schallmey A (2017). HheG, a halohydrin dehalogenase with activity on cyclic epoxides. ACS Catalysis 7, 6877-86

72.    von Tesmar A, Hoffmann M, Pippel J, Fayad AA, Dausend-Werner S, Bauer A, Blankenfeldt W, Müller R (2017). Total Biosynthesis of the Pyrrolo[4,2]benzodiazepine Scaffold Tomaymycin on an In Vitro Reconstituted NRPS System. Cell Chem Biol. 24:1216-27.

71.    Witzgall F, Erwert W, Blankenfeldt W (2017). Structures of the N-terminal domain of PqsA in complex with anthraniloyl- and 6-fluoroanthraniloyl-AMP: substrate activation in Pseudomonas Quinolone Signal (PQS) biosynthesis. Chembiochem 18:2045-55.

70.    Lukat P, Katsuyama Y, Wenzel S, Binz T, König C, Blankenfeldt W, Brönstrup M & Müller R (2017). Biosynthesis of methyl-proline containing griselimycins, natural products with anti-tuberculosis activity. Chem Sci. 8, 7521-7

69.    Diederich C#, Leypold M#, Culka M#, Weber HJ, Breinbauer R*, Ullmann GM* & Blankenfeldt W* (2017). Mechanisms and specificity of phenazine biosynthesis protein PhzF. Sci Rep. 7:6272. #equal contribution; *corresponding authors

68.    Bock T, Luxenburger E, Hoffmann J, Schütza V, Feiler C, Müller R & Blankenfeldt W (2017). AibA/AibB induces an intramolecular decarboxylation in de novo isovalerate biosynthesis of Myxococcus xanthus. Angew Chem Int Ed Engl. 56:9986-9

67.    Dolan SK, Bock T, Hering V, Owens RA, Jones GW, Blankenfeldt W*, Doyle S* (2017). Structural, mechanistic and functional insight into gliotoxin bis-thiomethylation in Aspergillus fumigatus. Open Biol. 7: 160292. * corresponding authors

66.    Bock T, Volz C, Hering V, Scrima A, Müller R, Blankenfeldt W (2017). The AibR-isovaleryl coenzyme A regulator and its DNA binding site - a model for the regulation of alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus.. Nucleic Acids Res. 45:2166-78.

65.    Bock T, Müller R & Blankenfeldt W (2016). Crystal structure of AibC, a reductase involved in alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus. Acta Crystallogr F72:652-8.

64.    Füller JJ, Röpke R, Krausze J, Rennhack KE, Daniel NP, Blankenfeldt W, Schulz S, Jahn D & Moser J (2016). Biosynthesis of Violacein, Structure and Function of l-Tryptophan Oxidase VioA from Chromobacterium violaceum. J. Biol. Chem. 291: 20068-84.

63.    Bock T, Reichelt J, Müller R & Blankenfeldt W (2016). The Structure of LiuC, a 3-Hydroxy-3-Methylglutaconyl CoA Dehydratase Involved in Isovaleryl-CoA Biosynthesis in Myxococcus xanthus, Reveals Insights into Specificity and Catalysis. Chembiochem 17:1658-64.

62.    Bock T#, Kasten J#, Müller R & Blankenfeldt W (2016). Crystal structure of the HMG-CoA synthase MvaS from the Gram-negative bacterium Myxococcus xanthus. Chembiochem 17:1257-62; #equal contribution

61.    Zender M, Witzgall F, Drees SL, Weidel E, Maurer CK, Fetzner S, Blankenfeldt W, Empting M* & Hartmann RW* (2016). Dissecting the Multiple Roles of PqsE in Pseudomonas aeruginosa Virulence by Discovery of Small Tool Compounds. ACS Chem Biol 11:1755-63; * corresponding authors

60.    Jiang W, Nowicki C* & Blankenfeldt W* (2015). Structural basis for the relaxed substrate selectivity of Leishmania mexicana broad specificity aminotransferase.  Mol Biochem Parasitol 202:34-7; *corresponding authors

59.    Vit A#, Mashabela GT#, Blankenfeldt W & Seebeck FP (2015). Structure of the ergothioneine-biosynthetic amidohydrolase EgtC. ChemBioChem 16:1490-6; #equal contribution

58.    Goncharenko KV#, Vit A#, Blankenfeldt W* & Seebeck FP* (2015). Structure of the sulfoxide synthase EgtB from the ergothioneine biosynthetic pathway. Angew Chem Int Ed Engl 54:2821-4. #equal contribution; *corresponding authors

57.    Vit A#, Misson L#, Blankenfeldt W & Seebeck FP (2015). Ergothioneine biosynthetic methyltransferase EgtD reveals the structural basis of aromatic amino acid betaine biosynthesis. ChemBioChem 16:119-25; #equal contribution

56.    Vit A, Misson L, Blankenfeldt W & Seebeck FP (2014). Crystallization and preliminary X-ray analysis of the ergothioneine-biosynthetic methyltransferase EgtD. Acta Cryst F70:676–680.

55.    Feiler C, Fisher AC, Marrichi MJ, Wright L, Schmidpeter PAM, Blankenfeldt W, Pavelka M, DeLisa MP (2013). Directed evolution of Mycobacterium tuberculosis beta-lactamase reveals gatekeeper residue that controls drug resistance and catalytic efficiency. PLoS ONE, 8:73123.

54.    Xu N, Ahuja EG, Janning P, Mavrodi DV, Thomashow LS, Blankenfeldt W (2013). Trapped intermediates in crystals of the FMN-dependent oxidase PhzG provide insight into the final steps of phenazine biosynthesis. Acta Cryst D69: 1403-13.

53.    Mavrodi DV, Parejko JA, Mavrodi OV, Kwak YS, Weller DM, Blankenfeldt W, Thomashow LS (2013). Recent insights into the diversity, frequency and ecological roles of phenazines in fluorescent Pseudomonas spp. Environ Microbiol 15:675-86.

52.    Hoeppner A, Thomas F, Rueppel A, Hensel R, Blankenfeldt W, Bayer P, Faust A (2012). Structure of the corrinoid:coenzyme M methyltransferase MtaA from Methanosarcina mazei. Acta Cryst D68:1549-57.

51.    Stigter EA, Guo Z, Bon RS, Wu YW, Choidas A, Wolf A, Menninger S, Waldmann H, Blankenfeldt W*, Goody RS* (2012). Development of Selective, Potent RabGGTase Inhibitors. J Med Chem 55:8830-40; *corresponding authors

50.    Xu N, Yu S, Moniot S, Weyand M, Blankenfeldt W (2012). Crystallization and preliminary crystal structure analysis of the ligand-binding domain of PqsR (MvfR), the Pseudomonas quinolone signal (PQS) responsive quorum-sensing transcription factor of Pseudomonas aeruginosa. Acta Cryst F68:1034-9.

49.    Deraeve C, Guo Z, Bon RS, Blankenfeldt W, Dilucrezia R, Wolf A, Menninger S, Stigter EA, Wetzel S, Choidas A, Alexandrov K, Waldmann H, Goody RS, Wu YW. (2012). Psoromic Acid is a Selective and Covalent Rab-Prenylation Inhibitor Targeting Autoinhibited RabGGTase. J Am Chem Soc 134:7384-91

48.    Mueller JW, Link NM, Matena A, Hoppstock L, Rüppel A, Bayer P, Blankenfeldt W (2011). Crystallographic proof for an extended hydrogen-bonding network in small prolyl isomerases. J Am Chem Soc 133:20096-9

47.    Bigalke JM, Dames SA, Blankenfeldt W, Grzesiek S, Geyer M (2011). Structure and dynamics of a stabilized coiled-coil domain in the P-TEFb regulator Hexim1. J Mol Biol 414:639-53

46.    Yu S, Vit A, Devenish S, Mahanty HK, Itzen A, Goody RS, Blankenfeldt W (2011). Atomic resolution structure of EhpR: phenazine resistance in Enterobacter agglomerans Eh1087 follows principles of bleomycin/mitomycin C resistance in other bacteria. BMC Struct Biol 11:33

45.    Waldmüller S, Erdmann J, Binner P, Gelbrich G, Pankuweit S, Geier C, Timmermann B, Haremza J, Perrot A, Scheer S, Wachter R, Schulze-Waltrup N, Dermintzoglou A, Schönberger J, Zeh W, Jurmann B, Brodherr T, Börgel J, Farr M, Milting H, Blankenfeldt W, Reinhardt R, Ozcelik C, Osterziel KJ, Loeffler M, Maisch B, Regitz-Zagrosek V, Schunkert H, Scheffold T (2011). Novel correlations between the genotype and the phenotype of hypertrophic and dilated cardiomyopathy: results from the German Competence Network Heart Failure. Eur J Heart Fail 13:1185-92

44.    Breuer S, Schievink SI, Schulte A, Blankenfeldt W, Fackler OT, Geyer M (2011). Molecular Design, Functional Characterization and Structural Basis of a Protein Inhibitor Against the HIV-1 Pathogenicity Factor Nef. PLoS ONE 6:e20033

43.    Bon RS, Guo Z, Stigter EA, Wetzel S, Menninger S, Wolf A, Choidas A, Alexandrov K, Blankenfeldt W, Goody RS, Waldmann H (2011). Structure-Guided Development of Selective RabGGTase Inhibitors. Angew Chem Int Ed Engl 50:4957-61

42.    Li QA, Mavrodi DV, Thomashow LS, Roessle M, Blankenfeldt W (2011). Ligand Binding Induces an Ammonia Channel in 2-Amino-2-desoxyisochorismate (ADIC) Synthase PhzE. J Biol Chem 286:18213-21

41.    Hou X, Hagemann N, Schoebel S, Blankenfeldt W, Goody RS, Erdmann KS, Itzen A (2011) A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1. EMBO J 30:1659-70

40.    Hoffjan S, Waldmüller S, Blankenfeldt W, Kötting J, Gehle P, Binner P, Epplen JT, Scheffold T. (2011) Three novel mutations in the ACTA2 gene in German patients with thoracic aortic aneurysms and dissections. Eur J Hum Gen 19:520-4

39.    Müller MP#, Peters H#, Blümer J, Blankenfeldt W*, Goody RS*, Itzen A*. (2010) The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. Science 329:946-9; #equal contribution; *corresponding authors

38.    Gazdag EM, Cirstea IC, Breitling R, Lukes J, Blankenfeldt W*, Alexandrov K*. (2010) Purification and crystallization of human Cu/Zn superoxide dismutase recombinantly produced in the protozoan Leishmania tarentolae. Acta Cryst F66:871-7; *corresponding authors

37.    Schoebel S, Blankenfeldt W, Goody RS, Itzen A. (2010) High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA. EMBO Rep 11:598-604

36.    Foldynová-Trantírková S, Sekyrová P, Tmejová K, Brumovská E, Bernatík O, Blankenfeldt W, Krejčí P, Kozubík A, Doležal T, Trantírek L, Bryja V. (2010) Breast cancer-specific mutations in CK1epsilon inhibit Wnt/beta-catenin and activate the Wnt/Rac1/JNK and NFAT pathways to decrease cell adhesion and promote cell migration. Breast Cancer Res 12:R30

35.    Mavrodi DV, Peever TL, Mavrodi OV, Parejko JA, Raaijmakers JM, Lemanceau P, Mazurier S, Heide L, Blankenfeldt W, Weller DM, Thomashow LS. (2010) Diversity and Evolution of the Phenazine Biosynthesis Pathway. Appl Environ Microbiol 76:866-79

34.    Schoebel S, Oesterlin LK, Blankenfeldt W, Goody RS, Itzen A (2009) RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity. Mol Cell 36:1060-72

33.    Tan KT, Guiu-Rozas E, Bon RS, Guo Z, Delon C, Wetzel S, Arndt S, Alexandrov K, Waldmann H, Goody RS, Wu YW, Blankenfeldt W (2009) Design, Synthesis and Characterization of Peptide-Based Rab Geranylgeranyl Transferase Inhibitors. J Med Chem 52:8025-37

32.    Mentel M, Blankenfeldt W*, Breinbauer R* (2009) The Active Site of an Enzyme Can Host Both Enantiomers of a Racemic Ligand Simultaneously. Angew Chem Int Ed Engl 48:9084-7; *corresponding authors

31.    Vollmuth F, Blankenfeldt W, Geyer M (2009) Structures of the dual bromodomains of the P-TEFb activating protein Brd4 at atomic resolution. J Biol Chem 284:36547-56

30.    Sychrovsky V, Foldynova-Trantirkova S, Spackova N, Robeyns K, Van Meervelt L, Blankenfeldt W, Vokacova Z, Sponer J, Trantirek L (2009) Revisiting the planarity of nucleic acid bases: Pyramidilization at glycosidic nitrogen in purine bases is modulated by orientation of glycosidic torsion. Nucleic Acids Res 37:7321-31

29.    Yu S, Jensen V, Seeliger J, Feldmann I, Weber S, Schleicher E, Häussler S, Blankenfeldt W (2009) Structure elucidation and preliminary assessment of hydrolase activity of PqsE, the Pseudomonas quinolone signal (PQS) response protein. Biochemistry 48:10298-307

28.    Nguyen UT, Guo Z, Delon C, Wu Y, Deraeve C, Fränzel B, Bon RS, Blankenfeldt W, Goody RS, Waldmann H, Wolters D, Alexandrov K (2009) Analysis of the eukaryotic prenylome by isoprenoid affinity tagging. Nat Chem Biol 5:227-35

27.    Bergbrede T, Chuky N, Schoebel S, Blankenfeldt W, Geyer M, Fuchs E, Goody RS, Barr F, Alexandrov K (2009) Biophysical analysis of the interaction of Rab6a GTPase with its effector domains. J Biol Chem 284:2628-35

26.    Ahuja EG, Janning P, Mentel M, Graebsch A, Breinbauer R, Hiller W, Costisella B, Thomashow LS, Mavrodi DV, Blankenfeldt W (2008) PhzA/B catalyzes formation of the tricyclic scaffold in phenazine biosynthesis. J Am Chem Soc 130:17053-61

25.    Guo Z, Wu YW, Das D, Delon C, Cramer J, Yu S, Thuns S, Lupilova N, Waldmann H, Brunsveld L, Goody RS, Alexandrov K,  Blankenfeldt W (2008) Structures of RabGGTase:substrate/product complexes provide insights into the evolution of protein prenylation. EMBO J 27:2444-56

24.    Guo Z, Wu YW, Tan KT, Bon R, Guio-Rozas E, Delon C, Wetzel S, Arndt S, Goody RS, Blankenfeldt W, Alexandrov K, Waldmann H (2008) Development of Selective RabGGTase Inhibitors and the First Crystal Structure of a RabGGTase Inhibitor Complex. Angew Chem Int Ed Engl 47:3747-57

23.    Budde BS, Binner P, Waldmüller S, Höhne W, Blankenfeldt W, Hassfeld S, Brömsen J, Dermintzoglu A, Wieczorek M, May E, Goody RS, Vosberg HP, Nürnberg P, Scheffold T (2007) A Novel Mutation in the ß-Myosin Heavy Chain Gene (MYH7) is Associated with Left Ventricular Non-Compaction in a Large German Family. PLoS ONE 2:e1362

22.    Blankenfeldt W*, Thomä NH, Wray JS, Gautel M, Schlichting I* (2006) Crystal structures of human cardiac b-myosin II S2-D provide insight into the functional role of the S2 subfragment. Proc Natl Acad Sci USA 103:17713-17; *corresponding authors

21.    Gohain N, Thomashow LS, Mavrodi DV, Blankenfeldt W (2006) The purification, crystallization and preliminary structural characterization of FAD-dependent monooxygenase PhzS, a phenzazine-modifying enzyme from Pseudomonas aeruginosa. Acta Cryst F62:989-92

20.    Gohain N, Thomashow LS, Mavrodi DV, Blankenfeldt W (2006) The purification, crystallization and preliminary structural characterization of PhzM, a phenazine-modifying methyltransferase from Pseudomonas aeruginosa. Acta Cryst F62:887-90

19.    Kühnel K, Blankenfeldt W, Terner J, Schlichting I (2006) Crystal structures of chloroperoxidase with its bound substrates and complexed with formate acetate and nitrate. J Biol Chem 281:23990-8

18.    Herde P, Blankenfeldt W (2006) The purification, crystallization and preliminary structural characterization of human MAWDBP a member of the phenazine biosynthesis-like protein family. Acta Cryst F62:546-9

17.    Blankenfeldt W, Kuzin AP, Skarina T, Korniyenko Y, Tong L, Bayer P, Janning P, Thomashow LS, Mavrodi DV (2004) Structure and function of the phenazine biosynthesis protein PhzF from Pseudomonas fluorescens. Proc Natl Acad Sci USA 101:16431-6

16.    Ahuja EG, Mavrodi DV, Thomashow LS, Blankenfeldt W (2004) Overexpression purification and crystallization of PhzA, the first enzyme of the phenazine biosynthesis pathway of Pseudomonas fluorescens 2-79. Acta Cryst D60:1129-31

15.    Mavrodi DV, Bleimling N, Thomashow LS, Blankenfeldt W (2004) The purification, crystallization and preliminary structural characterization of PhzF a key enzyme in the phenazine-biosynthesis pathway from Pseudomonas fluorescens 2-79. Acta Cryst D60:184-6

14.    Dong C, Major LL, Allen A, Blankenfeldt W, Maskell D, Naismith JH (2003) High-resolution structures of RmlC from Streptococcus suis in complex with substrate analogs locate the active site of this class of enzyme. Structure (Camb) 11:715-23

13.    Kerr ID, Wadsworth RIM, Cubeddu L, Blankenfeldt W, Naismith JH, White MF (2003) Insights into ssDNA recognition by the OB fold from a structural and thermodynamic study of Sulfolobus SSB. EMBO J 22:2561-70

12.    Blankenfeldt W, Kerr ID, Giraud MF, McMiken HJ, Leonard G, Whitfield C, Messner P, Graninger M, Naismith JH (2002) Variation on a theme of SDR: dTDP-6-deoxy-lyxo-4-hexulose reductase (RmlD) shows a new Mg2+-dependent dimerisation mode in a well-known enzyme family. Structure (Camb) 10:773-86

11.    Asuncion M*, Blankenfeldt W*, Barlow JN, Naismith JH (2002) Crystal structure of 3-methylaspartase from Clostridium tetanomorphum. J Biol Chem 277:8306-11; *equal contribution

10.    Kerr ID, Wadsworth RIM, Blankenfeldt W, Staines AG, White MF,  Naismith JH (2001) Over-expression purification crystallization and data collection of a single stranded DNA binding protein from Sulfolobus solfataricus. Acta Cryst D57:1290-2

9.      Asuncion M, Barlow JN, Pollard J, Staines AG, McMahon S, Blankenfeldt W, Gani D, Naismith JH (2001) Over-expression, purification, crystallization and data collection of 3-methylaspartase from Clostridium tetanomorphum. Acta Cryst D57:731-3

8.      Nowicki C, Hunter GR, Montmartini-Kalisz M, Blankenfeldt W, Hecht HJ, Kalisz H (2001) Recombinant tyrosine aminotransferase from Trypanosoma cruzi: Structural characterization and site directed mutagenesis of a broad substrate specificity enzyme. Biochim Biophys Acta 1564:268-81

7.      Blankenfeldt W, Asuncion M, Lam JS, Naismith JH (2000) The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA). EMBO J 19:6652-63

6.      Blankenfeldt W, Giraud MF, Leonard G, Rahim R, Creuzenet C, Lam JS, Naismith JH (2000) The purification, crystallisation and preliminary structural characterisation of glucose-1-phosphate thymidylyltransferase (RmlA), the first enzyme of the dTDP-L-rhamnose synthesis pathway from Pseudomonas aeruginosa. Acta Cryst D56:1501-4

5.      Blankenfeldt W, Nowicki C, Montemartini-Kalisz M, Kalisz HM, Hecht HJ (1999) Crystal structure of Trypanosoma cruzi tyrosine aminotransferase: substrate specificity is influenced by cofactor binding mod.e Protein Sci 8:2406-17

4.      Nowicki C, Montmartini M, Hunter GR, Blankenfeldt W, Kalisz H, Hecht HJ  (1998) Crystallization and preliminary X-ray analysis of tyrosine aminotransferase from Trypanosoma cruzi epimastigotes. Acta Cryst D54:105-7

3.      Völkel D, Blankenfeldt W, Schomburg D (1998) Large-scale production, purification and refolding of the full length prion protein from Syrian golden hamster in Escherichia coli using the glutathione S-transferase-fusion system. Eur J Biochem 251:462-71

2.      Blankenfeldt W, Liao JW, Lo LC, Yeh MCP (1996) Sequential Additions of Nucleophiles to Tricarbonyl(h4-cycloheptadienyl)iron Tetrafluoroborate. Tetrahedron Lett 37:7361-4

1.      Blankenfeldt W, Nokihara K, Naruse S, Lessel U, Schomburg D, Wray V (1996) NMR Spectroscopic Evidence That Helodermin, unlike Other Members of the Secretin/VIP Family of Peptides, Is Substantially Structured in Water. Biochemistry 35:5955-62


B. Reviews

9.      Guttenberger N, Blankenfeldt W, Breinbauer R. (2017) Recent developments in the isolation, biological function, biosynthesis, and synthesis of phenazine natural products. Bioorg Med Chem. 25:6149-66.

8.      Diederich C, Leypold M, Breinbauer R, Blankenfeldt W (2016) Aus zwei mach eins: die Biosynthese der Phenazine, BIOspektrum 22:137-9.

7.      Diederich C, Leypold M, Breinbauer R, Blankenfeldt W (2014) Die Biosynthese der Phenazine, Nachrichten aus der Chemie 62:975-80.

6.      Blankenfeldt W*, Parsons JF* (2014) The structural biology of phenazine biosynthesis. Curr Opin Struct Biol 29:26-33. *corresponding authors

5.      Itzen A, Blankenfeldt, W, Goody RS (2011) Adenylylation: renaissance of a forgotten post-translational modification. Trends Biochem Sci 36:221-8

4.      Goody RS, Müller MP, Schoebel S, Oesterlin LK, Blümer J, Peters H, Blankenfeldt, W, Itzen A (2011) The versatile Legionella effector protein DrrA. Commun Integ Biol 4:1-3

3.      Mentel M, Ahuja EG, Mavrodi CV, Breinbauer R, Thomashow LS, Blankenfeldt W (2009) Of Two Make One: The Biosynthesis of Phenazines. ChemBiochem 10:2295-304

2.      Mavrodi DV, Blankenfeldt W, Thomashow LS (2006) Phenazine Compounds in Fluorescent Pseudomonas spp.. Annu Rev Phytochemistry 44:417-45

1.      Dong C, Beis K, Giraud MF, Blankenfeldt W, Allard S, Major LL, Kerr ID, Whitfield C, Naismith JH (2003) A structural perspective on the enzymes that convert dTDP-D-glucose into dTDP-L-rhamnose. Biochem Soc Trans 31:532-6


Book Chapters:

3.      Blankenfeldt W (2013). The Biosynthesis of Phenazines. In: S. Chincholkar, L. Thomashow (eds.). Microbial Phenazines: Biosynthesis, Agriculture and Health. Springer:1-17.

2.      Alexandrov K, Wu YW, Blankenfeldt W, Waldmann H, Goody RS (2011). Organization and Function of the Rab Prenylation and Recycling Machinery. In: F. Tamanoi, C.A. Hrycyna, M.O. Bergo (eds.). The Enzymes, Vol. 29: Protein Prenylation PART A. Academic Press:147-62.

1.      Mavrodi DV, Thomashow L, Blankenfeldt W (2008) Biosynthesis and regulation of phenazine compounds in Pseudomonas spp. In: B. Rehm (ed.). Pseudomonas: Model Organism, Pathogen, Cell Factory. Wiley-VCH. Weinheim:331-52.



1.      Blankenfeldt W, Naismith JH (2001) Crystallisation and Functional Analysis of Glucose-1-phosphate Thymidylyltransferase (RmlA) from Pseudomonas aeruginosa. Patent WO/2002/006509


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    Bakterien ist jedes Mittel recht, um einen Organismus zu infizieren. Sie dringen in Zellen ein, wandern durch den Körper, täuschen das Immunsystem oder missbrauchen Abläufe der Wirtszelle für ihre Zwecke. Jedes Bakterium hat dabei seine eigene Methode. Welche Mechanismen Listeria-Bakterien nutzen, haben jetzt Strukturbiologen des Helmholtz-Zentrums für Infektionsforschung (HZI) in Braunschweig herausgefunden. Der Trick der Erreger: Sie binden mit zwei Invasionsproteinen an einen Rezeptor auf menschlichen Zellen und lassen sich in die Zelle einschleusen. Diese Eintrittskarte ist eigentlich für Faktoren reserviert, die das Zellwachstum und die Wundheilung steuern. Sehen Sie, wie Professor Dirk Heinz und seine Arbeitsgruppe den Bakterien auf die Spur gekommen sind…
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  • Video showing the mobility of PqsBC

    PqsBC exists in different conformational states. Computer simulations can be used to derive a dynamic mechanism from these states, in which PqsBC can bind to the fatty acid chain by closing the molecule.

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