PDBsum entry 3lq0

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protein ligands metals links
Hydrolase PDB id
Protein chain
235 a.a. *
GOL ×3
Waters ×300
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Zymogen structure of crayfish astacin metallopeptidase
Structure: Proastacin. Chain: a. Synonym: crayfish small molecule proteinase. Engineered: yes. Mutation: yes
Source: Astacus astacus. Broad-fingered crayfish. Organism_taxid: 6715. Expressed in: escherichia coli. Expression_system_taxid: 469008.
1.45Å     R-factor:   0.152     R-free:   0.180
Authors: T.Guevara,I.Yiallouros,R.Kappelhoff,S.Bissdorf,W.Stocker,F.X Ruth
Key ref: T.Guevara et al. (2010). Proenzyme structure and activation of astacin metallopeptidase. J Biol Chem, 285, 13958-13965. PubMed id: 20202938 DOI: 10.1074/jbc.M109.097436
08-Feb-10     Release date:   23-Feb-10    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P07584  (ASTA_ASTFL) -  Astacin
251 a.a.
235 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - Astacin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'.
      Cofactor: Zn(2+)
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     plasma membrane   3 terms 
  Biological process     negative regulation of binding of sperm to zona pellucida   6 terms 
  Biochemical function     hydrolase activity     8 terms  


DOI no: 10.1074/jbc.M109.097436 J Biol Chem 285:13958-13965 (2010)
PubMed id: 20202938  
Proenzyme structure and activation of astacin metallopeptidase.
T.Guevara, I.Yiallouros, R.Kappelhoff, S.Bissdorf, W.Stöcker, F.X.Gomis-Rüth.
Proteolysis is regulated by inactive (latent) zymogens, with a prosegment preventing access of substrates to the active-site cleft of the enzyme. How latency is maintained often depends on the catalytic mechanism of the protease. For example, in several families of the metzincin metallopeptidases, a "cysteine switch" mechanism involves a conserved prosegment motif with a cysteine residue that coordinates the catalytic zinc ion. Another family of metzincins, the astacins, do not possess a cysteine switch, so latency is maintained by other means. We have solved the high resolution crystal structure of proastacin from the European crayfish, Astacus astacus. Its prosegment is the shortest structurally reported for a metallopeptidase, and it has a unique structure. It runs through the active-site cleft in reverse orientation to a genuine substrate. Moreover, a conserved aspartate, projected by a wide loop of the prosegment, coordinates the zinc ion instead of the catalytic solvent molecule found in the mature enzyme. Activation occurs through two-step limited proteolysis and entails major rearrangement of a flexible activation domain, which becomes rigid and creates the base of the substrate-binding cleft. Maturation also requires the newly formed N terminus to be precisely trimmed so that it can participate in a buried solvent-mediated hydrogen-bonding network, which includes an invariant active-site residue. We describe a novel mechanism for latency and activation, which shares some common features both with other metallopeptidases and with serine peptidases.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21166898 N.Cerdà-Costa, T.Guevara, A.Y.Karim, M.Ksiazek, K.A.Nguyen, J.L.Arolas, J.Potempa, and F.X.Gomis-Rüth (2011).
The structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinases.
  Mol Microbiol, 79, 119-132.
PDB codes: 2xs3 2xs4
21233422 T.Goulas, J.L.Arolas, and F.X.Gomis-Rüth (2011).
Structure, function and latency regulation of a bacterial enterotoxin potentially derived from a mammalian adamalysin/ADAM xenolog.
  Proc Natl Acad Sci U S A, 108, 1856-1861.
PDB code: 3p24
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