17.09.2013, 17:00

Hans Brandstetter "Structural basis for activity regulation and substrate specificity in clostridial collagenases G, H and T"



Clostridial collagenases are among the most efficient enzymes to degrade collagen, by far the most predominant protein in man. In this presentation I will present crystal structures of three clostridial collagenase isoforms (ColG, ColH and ColT). The comparison of unliganded and liganded structures reveal a quaternary subdomain dynamics. In the unliganded ColH structure this globular dynamics is modulated by an aspartate switch motion that binds to the catalytic zinc. We further identified a calcium binding site in proximity to the catalytic zinc. Both ions are required for full activity, explaining why calcium critically affects the enzymatic activity of clostridial collagenases. Our studies further reveal that loops close to the active site thus serve as characteristic substrate selectivity filter. These elements explain the distinct peptidolytic and collagenolytic activities of these enzymes and provide a rational to engineer collagenases with customized substrate specificity as well as for inhibitor design.


Hans Brandstetter received a Ph.D. in chemistry summa cum laude from the Technical University of Munich in 1994. He conducted postdoctoral research at the Massachusetts Institute of Technology and Harvard Medical School, Cambridge/Boston, and Max-Planck-Institute, Martinsried. In 2003 he was appointed Chief Scientific Officer at proteros GmbH, Martinsried/Munich. Dr. Brandstetter was recruited to the University of Salzburg in 2005. Since 2012 he serves as the Head of the Department of Molecular Biology. My primary research interest is directed towards the structure, mechanism and regulation of proteolytic enzymes, in particular in the field of immunology, host-pathogen interaction and blood coagulation. Reflecting this interest, Hans Brandstetter is organizing an annual Winterschool on proteases with a more than 30 years tradition (www.uni-salzburg.at/tiers).


17.09.2013, 17:00


Saarland University

Building and room

Hall 02 in Bldg. B2.1


Johann Brandstetter,
Universität Salzburg


Dr. Rolf W. Hartmann

How to find us in Saarbrücken 

The HIPS building is located at the east entrance on the main campus of Saarland University, which is situated outside the city centre of Saarbrücken, the state capital of Saarland. Saarland is located in the south-west of Germany, having common frontiers with Luxembourg and France.


Helmholtz-Institut für Pharmazeutische Forschung Saarland (HIPS)
Universitätscampus E8 1
66123 Saarbrücken

By car

  • from the north (Cologne/Trier) via the motorway A1/A8 to „Autobahnkreuz Neunkirchen“, take A6 to „Saarbrücken“
  • from the east (Kaiserslautern/Mannheim) via A6 to "Saarbrücken/Paris"
  • from the north-west from Luxembourg via A620 by-pass the city centre and follow A6 to „Mannheim“
  • from the west (Metz/Paris) and south-west (Strasbourg) via the A4/A320 (E50) follow A6 (E50) to „Mannheim“
  • to reach the campus from motorway A6: take exit no. 5 „St. Ingbert West/Universität“, follow „Universität Ost“, (ca. 6 km)

By train

(ICE/TGV and Intercity - Saarbrücken Central Station) you can reach the campus by local busses from the main train station (112, 124) and the city centre (101, 102, 109, 111) within 15 min 
(see www.bahn.de)



PrintSend per emailShare