2Y3U
Crystal structure of apo collagenase G from Clostridium histolyticum at 2.55 Angstrom resolution
Summary for 2Y3U
| Entry DOI | 10.2210/pdb2y3u/pdb |
| Related | 2Y50 |
| Descriptor | COLLAGENASE, HEXAETHYLENE GLYCOL, CITRATE ANION, ... (5 entities in total) |
| Functional Keywords | hydrolase, gluzincin, metalloprotease |
| Biological source | CLOSTRIDIUM HISTOLYTICUM |
| Total number of polymer chains | 1 |
| Total formula weight | 90172.25 |
| Authors | Eckhard, U.,Brandstetter, H. (deposition date: 2010-12-26, release date: 2011-09-28, Last modification date: 2011-10-19) |
| Primary citation | Eckhard, U.,Schoenauer, E.,Nuess, D.,Brandstetter, H. Structure of Collagenase G Reveals a Chew-and -Digest Mechanism of Bacterial Collagenolysis Nat.Struct.Mol.Biol., 18:1109-, 2011 Cited by PubMed Abstract: Collagen constitutes one-third of body protein in humans, reflecting its extensive role in health and disease. Of similar importance, therefore, are the idiosyncratic proteases that have evolved for collagen remodeling. The most efficient collagenases are those that enable clostridial bacteria to colonize their host tissues; but despite intense study, the structural and mechanistic basis of these enzymes has remained elusive. Here we present the crystal structure of collagenase G from Clostridium histolyticum at 2.55-Å resolution. By combining the structural data with enzymatic and mutagenesis studies, we derive a conformational two-state model of bacterial collagenolysis, in which recognition and unraveling of collagen microfibrils into triple helices, as well as unwinding of the triple helices, are driven by collagenase opening and closing. PubMed: 21947205DOI: 10.1038/NSMB.2127 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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