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PDBsum entry 4fkc

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protein metals links
Hydrolase PDB id
4fkc
Jmol
Contents
Protein chain
370 a.a.
Metals
_CD ×12
Waters ×53
PDB id:
4fkc
Name: Hydrolase
Title: Recombinant prolidase from thermococcus sibiricus
Structure: Xaa-pro aminopeptidase. Chain: a. Engineered: yes
Source: Thermococcus sibiricus. Organism_taxid: 604354. Strain: mm 739 / dsm 12597. Gene: tsib_0821. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.60Å     R-factor:   0.233     R-free:   0.269
Authors: A.A.Trofimov,E.S.Slutskaya,K.M.Polyakov,P.V.Dorovatovskii, V.M.Gumerov,V.O.Popov
Key ref: A.A.Trofimov et al. (2012). Influence of intermolecular contacts on the structure of recombinant prolidase from Thermococcus sibiricus. Acta Crystallogr Sect F Struct Biol Cryst Commun, 68, 1275-1278. PubMed id: 23143231 DOI: 10.1107/S174430911203761X
Date:
13-Jun-12     Release date:   07-Nov-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
C6A2N7  (C6A2N7_THESM) -  Xaa-Pro aminopeptidase
Seq:
Struc:
365 a.a.
370 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

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

 

 
DOI no: 10.1107/S174430911203761X Acta Crystallogr Sect F Struct Biol Cryst Commun 68:1275-1278 (2012)
PubMed id: 23143231  
 
 
Influence of intermolecular contacts on the structure of recombinant prolidase from Thermococcus sibiricus.
A.A.Trofimov, E.A.Slutskaya, K.M.Polyakov, P.V.Dorovatovskii, V.M.Gumerov, V.O.Popov.
 
  ABSTRACT  
 
Prolidases are peptidases that are specific for dipeptides with proline as the second residue. The structure of recombinant prolidase from the hyperthermophilic archaeon Thermococcus sibiricus (Tsprol) was determined at 2.6 Å resolution. The homodimer of Tsprol is characterized by a complete lack of interactions between the N- and C-terminal domains of the two subunits and hence can be considered to be the most open structure when compared with previously structurally studied prolidases. This structure exists owing to intermolecular coordination bonds between cadmium ions derived from the crystallization solution and histidine residues of a His tag and aspartate and glutamate residues, which link the dimers to each other. This linking leads to the formation of a crystal with a loose packing of protein molecules and low resistance to mechanical influence and temperature increase.