2HLC
HL COLLAGENASE STRUCTURE AT 1.7A RESOLUTION
Summary for 2HLC
| Entry DOI | 10.2210/pdb2hlc/pdb |
| Descriptor | COLLAGENASE (2 entities in total) |
| Functional Keywords | serine protease, hydrolase, collagen degradation |
| Biological source | Hypoderma lineatum (early cattle grub) |
| Cellular location | Secreted: P08897 |
| Total number of polymer chains | 2 |
| Total formula weight | 50494.38 |
| Authors | Broutin, I.,Merigeau, K.,Arnoux, B.,Ducruix, A. (deposition date: 1997-01-08, release date: 1997-09-04, Last modification date: 2024-10-23) |
| Primary citation | Broutin, I.,Arnoux, B.,Riche, C.,Lecroisey, A.,Keil, B.,Pascard, C.,Ducruix, A. 1.8 A structure of Hypoderma lineatum collagenase: a member of the serine proteinase family. Acta Crystallogr.,Sect.D, 52:380-392, 1996 Cited by PubMed Abstract: Collagenase from the fly larvae Hypoderma lineatum cleaves triple-helical collagen in a single region. It was crystallized at neutral pH in the absence of inhibitor and 1.8 A data were collected using synchrotron radiation and a Mark II prototype detector. The structure was solved by combining multiple isomorphous replacement methods and rotation translation function in real space. Refinement between 7 and 1.8 A using the program X-PLOR led to a final R factor of 16.9%. The overall fold is similar to that of other trypsin-like enzymes but the structure differs mainly by the presence of a beta-sheet at position 31-44. The two embedded molecules of the asymmetric unit are related by a pseudo twofold axis. The beta-sheet 31-44 of one molecule is involved in hydrogen bonds with binding-pocket residues of the other molecule. It thus completely prevents access to the active site. The specificity of this enzyme probably results from the position of Phe192 and Tyr99 at the entrance of the active site. PubMed: 15299709DOI: 10.1107/S090744499501184X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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