1JF8

X-ray structure of reduced C10S, C15A arsenate reductase from pI258


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.12 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.208 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox duty.

Zegers, I.Martins, J.C.Willem, R.Wyns, L.Messens, J.

(2001) Nat Struct Biol 8: 843-847

  • DOI: https://doi.org/10.1038/nsb1001-843
  • Primary Citation of Related Structures:  
    1JF8, 1JFV

  • PubMed Abstract: 

    Arsenate reductase (ArsC) from Staphylococcus aureus plasmid pI258 plays a role in bacterial heavy metal resistance and catalyzes the reduction of arsenate to arsenite. The structures of the oxidized and reduced forms of ArsC were solved. ArsC has the PTPase I fold typical for low molecular weight tyrosine phosphatases (LMW PTPases). Remarkably, kinetic experiments show that pI258 ArsC also catalyzes the tyrosine phosphatase reaction in addition to arsenate reduction. These results provide evidence that ArsC from pI258 evolved from LMW PTPase by the grafting of a redox function onto a pre-existing catalytic site and that its evolutionary origin is different from those of arsenate reductases from Escherichia coli plasmid R773 and from Saccharomyces cerevisiae. The mechanism proposed here for the catalysis of arsenate reduction by pI258 ArsC involves a nucleophilic attack by Cys 10 on arsenate, the formation of a covalent intermediate and the transport of oxidative equivalents by a disulfide cascade. The reaction is associated with major structural changes in the ArsC.


  • Organizational Affiliation

    Dienst Ultrastruktuur, Vlaams interuniversitair Instituut voor Biotechnologie (VIB), Vrije Universiteit Brussel, Paardenstraat 65, B-1640 St. Genesius Rode, Belgium. igzegers@vub.ac.be


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
arsenate reductase131Staphylococcus aureusMutation(s): 2 
Gene Names: arsc
UniProt
Find proteins for P0A006 (Staphylococcus aureus)
Explore P0A006 
Go to UniProtKB:  P0A006
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A006
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.12 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.208 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 33.9α = 90
b = 34.2β = 90
c = 99.4γ = 90
Software Package:
Software NamePurpose
AMoREphasing
CNSrefinement
DENZOdata reduction
CCP4data scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-10-03
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-10-27
    Changes: Data collection, Database references, Derived calculations
  • Version 1.4: 2024-02-07
    Changes: Data collection