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PDBsum entry 3hdb

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protein ligands metals links
Hydrolase PDB id
3hdb
Jmol
Contents
Protein chain
417 a.a. *
Ligands
LYS-ASN-LEU
NAG-NAG
2PE ×4
Metals
_CL
_ZN
_CA ×7
Waters ×241
* Residue conservation analysis
PDB id:
3hdb
Name: Hydrolase
Title: Crystal structure of aahiv, a metalloproteinase from venom o agkistrodon acutus
Structure: Aahiv. Chain: a. Synonym: zinc metalloproteinase. Knl. Chain: l
Source: Agkistrodon acutus. Hundred-pace snake. Organism_taxid: 36307. Organism_taxid: 36307
Resolution:
2.31Å     R-factor:   0.214     R-free:   0.249
Authors: Z.Q.Zhu,L.W.Niu,M.K.Teng
Key ref: Z.Zhu et al. (2009). Structural basis of the autolysis of AaHIV suggests a novel target recognizing model for ADAM/reprolysin family proteins. Biochem Biophys Res Commun, 386, 159-164. PubMed id: 19505434 DOI: 10.1016/j.bbrc.2009.06.004
Date:
07-May-09     Release date:   11-Aug-09    
PROCHECK
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 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 417 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.24.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     proteolysis   1 term 
  Biochemical function     metallopeptidase activity     2 terms  

 

 
DOI no: 10.1016/j.bbrc.2009.06.004 Biochem Biophys Res Commun 386:159-164 (2009)
PubMed id: 19505434  
 
 
Structural basis of the autolysis of AaHIV suggests a novel target recognizing model for ADAM/reprolysin family proteins.
Z.Zhu, Y.Gao, Z.Zhu, Y.Yu, X.Zhang, J.Zang, M.Teng, L.Niu.
 
  ABSTRACT  
 
AaHIV, a P-III-type snake venom metalloproteinase (SVMP), consists of metalloproteinase/disintegrin/cysteine-rich (MDC) domains and is homologous to a disintegrin and metalloproteinase (ADAM) family proteins. Similar to brevilysin H6 and jararhagin, AaHIV can easily autolyse to release a stable protein named acucetin, which contains disintegrin-like and cysteine-rich domains. In this study, we determined the crystal structure of AaHIV and investigated the autolysis mechanism. Based on the structure of AaHIV and the results from docking experiments, we present a new model for target recognition in which two protein molecules form a functional unit, and the DC domain of one molecule is used for target recognition while the M-domain of the other is used for target proteolysis. Our results shed new light on the mechanism of target recognition and processing in ADAM/reprolysin family proteins.