PDBsum entry 4j4m

Hydrolase

PDB id: 4j4m

Contents

Protein chains

195 a.a.

Metals

_ZN ×6

Waters ×527

PDB id:

4j4m

Name:

Hydrolase

Title:

Crystal structure of tm-1, a trimeresurus mucrosquamatus venom metalloproteinase

Structure:

Zinc-dependent metalloproteinase. Chain: a, b. Ec: 3.4.24.53

Source:

Protobothrops mucrosquamatus. Taiwan habu. Organism_taxid: 103944

Resolution:

1.80Å R-factor: 0.184 R-free: 0.207

Authors:

T.L.Chou,C.H.Wu,K.F.Huang,A.H.Wang

Key ref:

T.L.Chou et al. (2013). Crystal structure of a Trimeresurus mucrosquamatus venom metalloproteinase providing new insights into the inhibition by endogenous tripeptide inhibitors. Toxicon, 71, 140-146. PubMed id: 23732127 DOI: 10.1016/j.toxicon.2013.05.009

Date:

07-Feb-13 Release date: 10-Jul-13

Protein chains

U3KRG1  (VM1T1_PROMU) -  Snake venom metalloproteinase TM-1 from Protobothrops mucrosquamatus

Seq: 202 a.a.

Struc: 195 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.24.- - ?????

DOI no: 10.1016/j.toxicon.2013.05.009

Toxicon 71:140-146 (2013)

PubMed id: 23732127

Crystal structure of a Trimeresurus mucrosquamatus venom metalloproteinase providing new insights into the inhibition by endogenous tripeptide inhibitors.

T.L.Chou, C.H.Wu, K.F.Huang, A.H.Wang.

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.