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PDBsum entry 3a52

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
3a52
Jmol
Contents
Protein chains
400 a.a. *
Ligands
SO4 ×3
Metals
_MG ×4
_ZN ×2
Waters ×801
* Residue conservation analysis
PDB id:
3a52
Name: Hydrolase
Title: Crystal structure of cold-active alkailne phosphatase from psychrophile shewanella sp.
Structure: Cold-active alkaline phosphatase. Chain: a, b. Engineered: yes
Source: Shewanella. Organism_taxid: 177958. Strain: ap1. Gene: scap. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.20Å     R-factor:   0.183     R-free:   0.244
Authors: H.Tsuruta,B.Mikami,T.Higashi,Y.Aizono
Key ref: H.Tsuruta et al. (2010). Crystal structure of cold-active alkaline phosphatase from the psychrophile Shewanella sp. Biosci Biotechnol Biochem, 74, 69-74. PubMed id: 20057143
Date:
24-Jul-09     Release date:   14-Apr-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8RQU7  (Q8RQU7_9GAMM) -  Cold-active alkaline phosphatase
Seq:
Struc:
398 a.a.
400 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   2 terms 
  Biochemical function     catalytic activity     3 terms  

 

 
Biosci Biotechnol Biochem 74:69-74 (2010)
PubMed id: 20057143  
 
 
Crystal structure of cold-active alkaline phosphatase from the psychrophile Shewanella sp.
H.Tsuruta, B.Mikami, T.Higashi, Y.Aizono.
 
  ABSTRACT  
 
The crystal structure of a cold-active alkaline phosphatase from a psychrophile, Shewanella sp. (SCAP), was solved at 2.2 A. A refined model showed a homodimer with six metal-ligand sites. The arrangement of the catalytic residues resembled those of alkaline phosphatases (APs), suggesting that the reaction mechanism of SCAP was fundamentally identical to those of other APs. SCAP had two distinct structural features: (i) a loop with Arg122 that bound to the phosphate moiety of the substrate suffered no constraints from the linkage to other secondary structures, and (ii) Mg3-ligand His109 was considered to undergo repulsive effect with neighboring Trp228. The local flexibility led by these features might be an important factor in the high catalytic efficiency of SCAP at low temperatures.