4J4M
Crystal structure of TM-1, a Trimeresurus mucrosquamatus venom metalloproteinase
Summary for 4J4M
| Entry DOI | 10.2210/pdb4j4m/pdb |
| Related | 1KUF |
| Descriptor | zinc-dependent metalloproteinase, ZINC ION (3 entities in total) |
| Functional Keywords | alpha/beta-mixed fold, endopeptidase, hydrolase |
| Biological source | Protobothrops mucrosquamatus (Taiwan habu) |
| Total number of polymer chains | 2 |
| Total formula weight | 44011.74 |
| Authors | Chou, T.L.,Wu, C.H.,Huang, K.F.,Wang, A.H. (deposition date: 2013-02-07, release date: 2013-07-10, Last modification date: 2024-11-06) |
| Primary citation | Chou, T.L.,Wu, C.H.,Huang, K.F.,Wang, A.H. Crystal structure of a Trimeresurus mucrosquamatus venom metalloproteinase providing new insights into the inhibition by endogenous tripeptide inhibitors. Toxicon, 71C:140-146, 2013 Cited by PubMed Abstract: The crystal structure of TM-1, a P-I class snake-venom metalloproteinase (SVMP) from the Trimeresurus mucrosquamatus venom, was determined at 1.8-Å resolution. The structure exhibits the typical feature of SVMPs and is stabilized by three disulfide linkages. The active site shows a deep S1' substrate-binding pocket limited by the non-conserved Pro174 at the bottom. Further comparisons with other SVMPs suggest that the deep S1' site of TM-1 correlates with its high inhibition sensitivity to the endogenous tripeptide inhibitors. Proteolytic specificity analysis revealed that TM-1 prefers substrates having a moderate-size and hydrophobic residue at the P1' position, consistent with our structural observation. PubMed: 23732127DOI: 10.1016/j.toxicon.2013.05.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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