Structure and Function of Proteins

The staff in the field of Structural Biology investigates the spatial structure and function of individual molecules. In this they utilise modern technologies such as x-ray structure analysis, nuclear magnetic resonance spectroscopy (NMR) and mass spectrometry. Analysis is undertaken of both biomacromolecules (peptides, proteins, nucleic acids, etc.) and low molecular natural substances.

Publications of Dirk Heinz

  • Storbeck,S.; Saha,S.; Krausze,J.; Klink,B.U.; Heinz,Dirk W.*; Layer,G.; (2011). Crystal Structure of the Heme d1 Biosynthesis Enzyme NirE in Complex with Its Substrate Reveals New Insights into the Catalytic Mechanism of S-Adenosyl-L-methionine-dependent Uroporphyrinogen III Methyltransferases. Journal of Biological Chemistry: 286 30, 26754-26767 DOI: 10.1074/jbc.M111.239855 HZI repository PubMed
  • Wilke,S.; Gröbe,Lothar*; Maffenbeier,V.; Jäger,Volker*; Gossen,M.; Josewski,J.; Duda,A.; Polle,L.; Owens,R.J.; Wirth,Dagmar*; Heinz,Dirk* W.; van den,Heuvel Joop*; Büssow,Konrad*; (2011). Streamlining homogeneous glycoprotein production for biophysical and structural applications by targeted cell line development. PLoS ONE: 6 12, e27829 DOI: 10.1371/journal.pone.0027829 HZI repository PubMed
  • de Groot,J.C.; Schluter,K.; Carius,Y.; Quedenau,C.; Vingadassalom,D.; Faix,J.; Weiss,S.M.; Reichelt,J.; Standfuss-Gabisch,C.; Lesser,C.F.; Leong,J.M.; Heinz,Dirk W.*; Büssow,Konrad*; Stradal,Theresia E.*; (2011). Structural Basis for Complex Formation between Human IRSp53 and the Translocated Intimin Receptor Tir of Enterohemorrhagic E. coli. 19 9, 1294-1306 DOI: 10.1016/j.str.2011.06.015 HZI repository PubMed
  • Quade,N.; Dieckmann,M.; Haffke,M.; Heroven,A.K.; Dersch,Petra*; Heinz,Dirk W.*; (2011). Structure of the effector-binding domain of the LysR-type transcription factor RovM from Yersinia pseudotuberculosis. Acta Crystallographica Section D: Biological Crystallography: 67 Pt 2, 81-90 DOI: 10.1107/S0907444910049681 HZI repository PubMed
  • Quade,N.; Huo,L.; Rachid,S.; Heinz,Dirk W.*; Müller,Rolf*; (2011). Unusual carbon fixation gives rise to diverse polyketide extender units. Nature Chemical Biology: 8 1, 117-124 PubMed
  • Brocker,M.J.; Schomburg,S.; Heinz,Dirk W.*; Jahn,D.; Schubert,W.D.; Moser,J.; (2010). Crystal structure of the nitrogenase-like dark operative protochlorophyllide oxidoreductase catalytic complex (ChlN/ChlB)2. Journal of Biological Chemistry: 285 35, 27336-27345 PubMed
  • Heinz,Dirk W.*; Betzel,C.; Wilmanns,M.; (2010). Highlight: of systems and structures. Biological Chemistry: 391 7, 717-718 PubMed
  • Ferraris,D.M.; Gherardi,E.; Di,Y.; Heinz,Dirk W.*; Niemann,H; (2010). Ligand-mediated dimerization of the Met receptor tyrosine kinase by the bacterial invasion protein InIB. Journal of Molecular Biology: 395 3, 522-532 DOI: 10.1016/j.jmb.2009.10.074 HZI repository PubMed
  • Layer,G.; Reichelt,J.; Jahn,D.; Heinz,Dirk W.*; (2010). Structure and function of enzymes in heme biosynthesis. Protein Science: 19 6, 1137-1161 PubMed
  • Klink,B.U.; Barden,S.; Heidler,T.V.; Borchers,C.; Ladwein,M.; Stradal,Theresia B.*; Rottner,Klemens*; Heinz,Dirk W.*; (2010). Structure of Shigella IpgB2 in complex with human RhoA: implications for the mechanism of bacterial guanine nucleotide exchange factor mimicry. Journal of Biological Chemistry: 285 22, 17197-17208 DOI: 10.1074/jbc.M110.107953 HZI repository PubMed
  • Heinemann,I.U.; Schulz,C.; Schubert,W.D.; Heinz,Dirk W.*; Wang,Y.G.; Kobayashi,Y.; Awa,Y.; Wachi,M.; Jahn,D.; Jahn,M.; (2010). Structure of the heme biosynthetic Pseudomonas aeruginosa porphobilinogen synthase in complex with the antibiotic alaremycin. Antimicrobial Agents and Chemotherapy: 54 1, 267-272 PubMed
  • Haffke,M.; Menzel,A.; Carius,Y.; Jahn,D.; Heinz,Dirk W.*; (2010). Structures of the nucleotide-binding domain of the human ABCB6 transporter and its complexes with nucleotides. Acta Crystallographica Section D: Biological Crystallography: 66 Pt 9, 979-987 PubMed
  • Rand,K.; Noll,C.; Schiebel,H.M.; Kemken,D.; Dulcks,T.; Kalesse,Markus*; Heinz,Dirk W.*; Layer,G.; (2010). The oxygen-independent coproporphyrinogen III oxidase HemN utilizes harderoporphyrinogen as a reaction intermediate during conversion of coproporphyrinogen III to protoporphyrinogen IX. Biological Chemistry: 391 1, 55-63 PubMed
  • Marin,M.; Heinz,Dirk W.*; Pieper,Dietmar H.*; Klink,B.U.; (2009). Crystal structure and catalytic mechanism of 4-methylmuconolactone methylisomerase. Journal of Biological Chemistry: 284 47, 32709-32716 PubMed
  • Bublitz,M.; Nimtz,Manfred*; Polle,L.; Holland,C.; Heinz,Dirk W.*; Schubert,Wolf-Dieter*; (2009). Structural basis for autoinhibition and activation of Auto, a virulence-associated peptidglycan hydrolase of L. monocytogenes. Molecular Microbiology: 71 6, 1509-1522
  • Wiesand,U.; Sorg,I.; Amstutz,M.; Wagner,S.; van den Heuvel,Joop*; Lührs,Thorsten*; Cornelis,G.R.; Heinz,Dirk W.*; (2009). Structure of the type III secretion recognition protein YscU from Yersinia enterocolitica. Journal of Molecular Biology: 385 3, 854-866 DOI: 10.1016/j.jmb.2008.10.034 HZI repository PubMed
  • Brocker,M.J.; Virus,S.; Ganskow,S.; Heathcote,P.; Heinz,Dirk W.*; Schubert,W.D.; Jahn,D.; Moser,J.; (2008). ATP-driven reduction by dark-operative protochlorophyllide oxidoreductase from Chlorobium tepidum mechanistically resembles nitrogenase catalysis. Journal of Biological Chemistry: 283 16, 10559-10567 PubMed
  • Buettner,C.R.; Sorg,I.; Cornelis,G.R.; Heinz,D.W.; Niemann,H.H.; (2008). Structure of the Yersinia enterocolitica type III secretion translocator chaperone SycD. Journal of Molecular Biology: 375 4, 997-1012 DOI: 10.1016/j.jmb.2007.11.009 HZI repository PubMed
  • Wendt,K.U.; Weiss,M.S.; Cramer,P.; Heinz,Dirk W.*; (2008). Structures and diseases. Nature Structural and Molecular Biology: 15 2, 117-120 DOI: 10.1038/nsmb0208-117 HZI repository PubMed
  • Niemann,H.H.; Petoukhov,M.V.; Hartlein,M.; Moulin,M.; Gherardi,E.; Timmins,P.; Heinz,D.W.; Svergun,D.I.; (2008). X-ray and neutron small-angle scattering analysis of the complex formed by the met receptor and the Listeria monocytogenes invasion protein InlB. Journal of Molecular Biology: 377 2, 489-500 DOI: 10.1016/j.jmb.2008.01.027 HZI repository PubMed
  • Hagelüken,G.; Wiehlmann,L.; Adams,T.M.; Kolmar,H.; Heinz,Dirk W.*; Tümmler,B.; Schubert,Wolf-Dieter*; (2007). Crystal structure of the electron transfer complex rubredoxin-rubredoxin reductase of Pseudomonas aeruginosa. Proceedings of the National Academy of Sciences of the United States of America (PNAS): 104 30, 12276-12281 DOI: 10.1073/pnas.0702919104 HZI repository PubMed
  • Wollert,T.; Pasche,Bastian*; Rochon,Maike*; Deppenmeier,S.; van den Heuvel,Joop*; Gruber,A.D.; Heinz,Dirk W.*; Lengeling,Andreas*; Schubert,Wolf-Dieter*; (2007). Extending the host range of Listeria monocytogenes by rational protein design. Cell: 129 5, 891-902
  • Lüer,C.; Schauer,S.; Virus,S.; Schubert,Wolf-Dieter*; Heinz,Dirk W.*; Jahn,D.; Moser,J.; (2007). Glutamate recognition and hydride transfer by Escherichia coli glutamyl-tRNA reductase. FEBS Journal: 274 17, 4609-4614 DOI: 10.1111/j.1742-4658.2007.05989.x HZI repository PubMed
  • Niemann,H.N.; Jäger,Volker*; Butler,P.J.G.; van den Heuvel,Joop*; Schmidt,S.; Ferraris,D.; Gherardi,E.; Heinz,Dirk W.*; (2007). Structure of the human receptor tyrosine kinase met in complex with the Listeria monocytogenes Invasion Protein InlB. Cell: 130 2, 235-246 DOI: 10.1016/j.cell.2007.05.037 HZI repository PubMed
  • Wollert,Thomas*; Heinz,Dirk W.*; Schubert,Wolf-Dieter*; (2007). Thermodynamically reengineering the listerial invasion complex InIA/E-Cadherin. Proceedings of the National Academy of Sciences of the United States of America (PNAS): 104 35, 13960-13965 DOI: 10.1073/pnas.0702199104 HZI repository PubMed
  • Heinz,Dirk W.*; Weiss,M.S.; Wendt,K.U.; (2006). Biomacromolecular interactions, assemblies and machines: A structural view. ChemBioChem: 7 203, 208 DOI: 10.1002/cbic.200500459 HZI repository PubMed
  • Schulze,J.O.; Masoumi,A.; Nickel,D.; Jahn,M.; Schubert,Wolf-Dieter*; Heinz,Dirk W.*; (2006). Crystal structure of a non-discriminating glutamyl-tRNA synthetase. Journal of Molecular Biology: 361, 888-897 DOI: 10.1016/j.jmb.2006.06.054 HZI repository PubMed
  • Schulze,J.O.; Schubert,Wolf-Dieter*; Moser,J.; Jahn,D.; Heinz,Dirk W.*; (2006). Evolutionary relationship between initial enzymes of tetrapyrrole biosynthesis. Journal of Molecular Biology: 358, 1212-1220 DOI: 10.1016/j.jmb.2006.02.064 HZI repository PubMed
  • Frese,S.; Schubert,Wolf-Dieter*; Findeis,A.C.; Marquardt,T.; Roske,Y.S.; Stradal,Theresia E.B.*; Heinz,Dirk W.*; (2006). Phosphotyrosine binding specificities of Nck1 and Nck2. Journal of Biological Chemistry: 281, 18236-18245
  • Frere,F.; Nentwich,M.; Gacond,S.; Heinz,Dirk W.*; Neier,R.; Frankenberg-Dinkel,N.; (2006). Probing the active site of Pseudomonas aeruginosa porphobilinogen synthase using newly developed inhibitors. Biochemistry: 45, 8243-8253
  • Hagelüken,G.; Adams,T.M.; Wiehlmann,L.; Widow,Ute*; Kolmar,H.; Tümmler,B.; Heinz,Dirk W.*; Schubert,Wolf-Dieter*; (2006). The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa , defines an independent, third mechnanistic class of sulfatases. Proceedings of the National Academy of Sciences of the United States of America (PNAS): 103, 7631-7636
  • Layer,G.; Pierik,A.J.; Trost,M.; Jänsch,Lothar*; Leech,H.K.; Warren,M.J.; Rigby,S.E.; Astner,I.; Grage,K.; Breckau,D.; Heinz,Dirk W.*; Jahn,D.; (2006). The substrate radical of Escherichia coli oxygen-independent coproporphyrinogen III oxidase HemN. Journal of Biological Chemistry: 281, 15727-15734
  • Jahn,D.; Moser,J.; Schubert,Wolf-Dieter*; Heinz,Dirk W.*; (2006). Transfer RNA-dependent aminolevulinic acid formation: structure and function of glutamyl-tRNA synthase, reductase and glutamate-1-semialdehyde-2,1-aminomutase.: Chlorophylls and Bacteriochlorophylls: Biochemistry, Biophysics, Functions and Applications. Grimm,B.; Porra,R.J.; Rudiger,W.; Scheer,H.; (Ed.). Dordrecht : Springer Verlag, 159-171
  • Reichelt,J.; Dieterich,G.; Kvesic,M.; Schomburg,D.; Heinz,D.W.; (2005). BRAGI. Linking and visualization of database information in a 3D-viewer and modelling tool. Bioinformatics: 21, 1291-1293
  • Lüer,C.; Schauer,S.; Möbius,K.; Schulze,J.; Schubert,W.-D.; Heinz,D.W.; Jahn,D.; Moser,J.; (2005). Complex formation between Glutamyl-tRNA Reductase and Glutamate-1-semialdehyde-2,1-aminomutase in Escherichia coli during the initial reactions of porphyrin biosynthesis. Journal of Biological Chemistry: 280, 18568-18572
  • Astner,I.; Schulze,J.O.; van den Heuvel,J.; Jahn,D.; Schubert,W.-D.; Heinz,D.W.; (2005). Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans. Embo Journal: 24, 3166-3177 DOI: 10.1038/sj.emboj.7600792 HZI repository
  • Buettner,C.; Cornelis,G.R.; Heinz,D.W.; Niemann,H.H.; (2005). Crystal structure of Yersinia enterocolitica. Protein Science: 14, 1993-2002
  • Heinz,D.W.; Schubert,W.-D.; Höfle,G.; (2005). Much anticipated - The bioactive conformation of epothilone and its binding to tubulin. Angewandte Chemie - International Edition: 44, 1298-1301
  • Heinz,D.W.; Schubert,W.-D.; (2005). Proteins in motion. Angewandte Chemie - International Edition: 44, 4428
  • Layer,G.; Kervio,E.; Morlock,G.; Heinz,D.W.; Jahn,D.; Retey,J.; Schubert,W.-D.; (2005). Structural and functional comparison of HemN to other radical SAM enzymes. Biological Chemistry: 386, 971-980
  • Eiting,M.; Hagelüken,G.; Schubert,W.-D.; Heinz,D.W.; (2005). The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes , increases DNA-binding affinity by stabilizing the HTH-motif. Molecular Microbiology: 56 2, 433-446
  • Frere,F.; Reents,H.; Schubert,W.-D.; Heinz,D.W.; (2005). Tracking the evolution of porphobilinogen synthase metal dependence in vitro. Journal of Molecular Biology: 345 5, 1059-1070
  • Niemann,H.; Schubert,W.-D.; Heinz,D.; (2004). Adhesins and invasions of pathogenic bacteria: a structural view. Microbes and Infection: 6, 101-112
  • Freiberg,A.; Machner,M-P.; Pfeil,W.; Schubert,W.-D.; Heinz,D.W.; Seckler,R.; (2004). Folding and stability of the leucine-rich repeat domain of internalin B from Listeria monocytogenes. Journal of Molecular Biology: 337 2, 453-461
  • Dieterich,G.; Kvesic,M.; Schomburg,D.; Heinz,D.W.; Reichelt,J.; (2004). Integrating public databases into an existing protein visualization and modeling program BRAGI. Lecture Notes in Informatics: P-53, 149-156
  • Ehinger,S.; Schubert,W.-D.; Bergmann,S.; Hammerschmidt,S.; Heinz,D.W.; (2004). Plasmin(ogen)-binding alpha-Enolase from Streptococcus pneumoniae : crystal structure and evaluation of plasmin(ogen)-binding sites. Journal of Molecular Biology: 343, 997-1005
  • Layer,G.; Heinz,D.W.; Jahn,D.; Schubert,W.-D.; (2004). Structure and function of radical SAM enzymes. Current Opinion in Chemical Biology: 8, 468-476
  • Machner,M.P.; Frese,S.; Schubert,W.-D.; Orian-Rousseau,V.; Gherardi,E.; Wehland,J.; Niemann,H.H.; Heinz,D.W.; (2003). Aromatic amino acids at the surface of In1B are essential for host cell invasion by Lysteria monocytogenes. Molecular Microbiology: 48, 1525-1536
  • Schubert,W.-D.; Heinz,D.W.; (2003). Details der Wechselwirkung zwischen Bakterium und Mensch. Laborwelt: 1, 16
  • Heesemann,J.; Heinz,D.W.; Rüssmann,H.; Wehland,J.; Goebel,W.; Kuhn,M.; (2003). Lektionen aus der Bakterienwelt: Ausnutzung von Wirtszellprozessen durch pathogene Mikroben. Biospektrum: 9, 486-489
  • Schubert,W.-D.; Heinz,D.W.; (2003). Structural aspects of adhesion and invasion of host cells by the human pathogen Listeria monocytogenes. ChemBioChem: 4, 1285-1291
  • van den Heuvel,J.; Heinz,D.W.; (2002). "Plug and Play"-expression systems for high-quality production of recombinant proteins for structural analysis. Gene Function & Disease: 3 1/2, 33-38
  • Schauer,S.; Chaturvedi,S.; Randau,L.; Moser,J.; Kitabatake,M.; Lorenz,S.; Verkamp,E.; Schubert,W.-D.; Nakayashiki,T.; Murai,M.; Wall,K.; Thomann,U.; Heinz,D.W.; Inokuchi,H.; Söll,D.; Jahn,D.; (2002). Escherichia coli glutamyl-tRNA reductase: trapping the thioester intermediate.. Journal of Biological Chemistry: 247 50, 48656-48663
  • Heinz,D.W.; (2002). Modellsystem für Infektionen - Pathogene Bakterien auf ihrem unheilvollen Weg verfolgt. Jahreshefte der Helmholtz-Gesellschaft:, 10-11
  • Schubert,W.D.; Moser,J.; Schauer,S.; Heinz,D.W.; Jahn,D.; (2002). Structure and function of glutamyl-tRNA reductases, the first enzyme of tetrapyrrole biosynthesis in plants and prokaryotes. Photosynthesis Research: 74, 205-215
  • Moser,J.; Schubert,W.-D.; Heinz,D.W.; Jahn,D.; (2002). Structure and function of glutamyl-tRNA-reductase involved in 5-aminolevulinic acid formation. Biochemical Society Transactions: 30, 579-584
  • Frere,F.; Schubert,W.-D.; Neier,R.; Jahn,D.Heinz D.W.; (2002). Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism. Journal of Molecular Biology: 320, 237-247
  • Schubert,W.-D.; Urbanke,C.; Ziehm,T.; Beier,V.; Machner,M.P.; Domann,E.; Wehland,J.; Chakraborty,T.; Heinz,D.W.; (2002). Structure of the complex of internalin, a major invasion protein of Listeria monocytogenes with its human receptor, E-cadherin.. Cell: 111, 825-836
  • Heinz,D.W.; Jahn,D.; (2002). Strukturbiologie zur gerichteten Wirkstoffentwicklung. CHEManager: 11, 14
  • Schubert,W.D.; Göbel,G.; Diepholz,M.; Darji,A.; Kloer,D.; Hain,T.; Chakraborty,T.; Wehland,J.; Domann,E.; Heinz,D.W.; (2001). Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain. Journal of Molecular Biology: 312 4, 783-7940022-2836 PubMed
  • Barzik,M.; Carl,U.D.; Schubert,W.D.; Frank,R.; Wehland,J.; Heinz,D.W.; (2001). The N-terminal domain of Homer/Vesl is a new class II EVH1 domain. Journal of Molecular Biology: 309 1, 155-1690022-2836 PubMed
  • Moser,J.; Schubert,W.D.; Beier,V.; Bringemeier,I.; Jahn,D.; Heinz,D.W.; (2001). V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA- dependent tetrapyrrole biosynthesis. Embo Journal: 20 23, 6583-65900261-4189 PubMed
  • Barzik,M.; Schubert,W.D.; Carl,U.; Wehland,J.; Heinz,D.W.; (2000). Crystallization and preliminary X-ray analysis of the EVH1 domain of Vesl-2b. 56 7, 930-9320907-4449 DOI: 10.1107/S0907444900005758 Full text HZI repository PubMed



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  • Doppelt aktiviert besser
    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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