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PDBsum entry 3lq0

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protein ligands metals links
Hydrolase PDB id
3lq0
Jmol
Contents
Protein chain
235 a.a. *
Ligands
GOL ×3
SO4
Metals
_ZN
Waters ×300
* Residue conservation analysis
PDB id:
3lq0
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.
Resolution:
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
Date:
08-Feb-10     Release date:   23-Feb-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P07584  (ASTA_ASTFL) -  Astacin
Seq:
Struc:
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.3.4.24.21  - 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.
 
  ABSTRACT  
 
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
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.