PDBsum entry 1shq

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
476 a.a. *
NAG ×2
SO4 ×4
_ZN ×4
_MG ×2
Waters ×102
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Crystal structure of shrimp alkaline phosphatase with magnes
Structure: Alkaline phosphatase. Chain: a, b. Ec:
Source: Pandalus borealis. Northern shrimp. Organism_taxid: 6703
Biol. unit: Dimer (from PQS)
2.00Å     R-factor:   0.216     R-free:   0.238
Authors: M.M.E.De Backer,S.Mcsweeney,P.F.Lindley,E.Hough
Key ref: Backer et al. (2004). Ligand-binding and metal-exchange crystallographic studies on shrimp alkaline phosphatase. Acta Crystallogr D Biol Crystallogr, 60, 1555-1561. PubMed id: 15333925 DOI: 10.1107/S0907444904015628
26-Feb-04     Release date:   31-Aug-04    
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Protein chains
Pfam   ArchSchema ?
Q9BHT8  (Q9BHT8_PANBO) -  Alkaline phosphatase (Fragment)
475 a.a.
476 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Alkaline phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: A phosphate monoester + H2O = an alcohol + phosphate
phosphate monoester
+ H(2)O
= alcohol
+ phosphate
      Cofactor: Mg(2+); Zn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   2 terms 
  Biochemical function     catalytic activity     5 terms  


DOI no: 10.1107/S0907444904015628 Acta Crystallogr D Biol Crystallogr 60:1555-1561 (2004)
PubMed id: 15333925  
Ligand-binding and metal-exchange crystallographic studies on shrimp alkaline phosphatase. Backer, S.McSweeney, P.F.Lindley, E.Hough.
Alkaline phosphatases (APs) are homodimeric metalloenzymes that catalyze the hydrolysis and transphosphorylation of phosphate monoesters. Each monomer contains a metal-binding triad that for optimal activity is usually occupied by two zinc ions and one magnesium ion. The recently determined crystal structure of cold-active shrimp alkaline phosphatase (SAP) was, however, fully occupied by zinc ions. This paper describes a metal-exchange experiment in which the zinc ion in one binding site (referred to as the M3 site) is replaced by magnesium. Crystal structures revealed a concomitant structural change: the metal exchange causes movement of a ligating histidine into a conformation in which it does not coordinate to the metal ion. The M3 site is relevant to catalysis: its occupation by magnesium is postulated to favour catalysis and it has been suggested to be a regulatory site for other APs. Further crystallographic studies show that ligand binding can induce a conformational change of an active-site arginine from a 'non-docked' (non-interacting) to a 'docked' conformation (interacting with the ligand). The first conformation has only been observed in SAP, while the latter is common in available AP structures. The observation that the arginine does not always bind the substrate may explain the increased catalytic efficiency that is generally observed for cold-active enzymes.
  Selected figure(s)  
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2004, 60, 1555-1561) copyright 2004.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
17311351 D.Chen, G.Menche, T.D.Power, L.Sower, J.W.Peterson, and C.H.Schein (2007).
Accounting for ligand-bound metal ions in docking small molecules on adenylyl cyclase toxins.
  Proteins, 67, 593-605.  
16815919 P.Llinas, M.Masella, T.Stigbrand, A.Ménez, E.A.Stura, and M.H.Le Du (2006).
Structural studies of human alkaline phosphatase in complex with strontium: implication for its secondary effect in bones.
  Protein Sci, 15, 1691-1700.
PDB code: 2glq
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