1RXE

ArsC complexed with MNB


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.212 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.196 

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This is version 1.3 of the entry. See complete history


Literature

The structure of a triple mutant of pI258 arsenate reductase from Staphylococcus aureus and its 5-thio-2-nitrobenzoic acid adduct.

Messens, J.Van Molle, I.Vanhaesebrouck, P.Van Belle, K.Wahni, K.Martins, J.C.Wyns, L.Loris, R.

(2004) Acta Crystallogr D Biol Crystallogr 60: 1180-1184

  • DOI: https://doi.org/10.1107/S0907444904007334
  • Primary Citation of Related Structures:  
    1RXE, 1RXI

  • PubMed Abstract: 

    Structural insights into formation of the complex between the ubiquitous thiol-disulfide oxidoreductase thioredoxin and its oxidized substrate are under-documented owing to its entropical instability. In vitro, it is possible via a reaction with 5,5'-dithiobis-(2-nitrobenzoic acid) to make a stable mixed-disulfide complex between thioredoxin from Staphylococcus aureus and one of its substrates, oxidized pI258 arsenate reductase (ArsC) from S. aureus. In the absence of the crystal structure of an ArsC-thioredoxin complex, the structures of two precursors of the complex, the ArsC triple mutant ArsC C10SC15AC82S and its 5-thio-2-nitrobenzoic acid (TNB) adduct, were determined. The ArsC triple mutant has a structure very similar to that of the reduced form of wild-type ArsC, with a folded redox helix and a buried catalytic Cys89. In the adduct form, the TNB molecule is buried in a hydrophobic pocket and the disulfide bridge between TNB and Cys89 is sterically inaccessible to thioredoxin. In order to form a mixed disulfide between ArsC and thioredoxin, a change in the orientation of the TNB-Cys89 disulfide in the structure is necessary.


  • Organizational Affiliation

    Laboratorium voor Ultrastructuur, Vlaams Interuniversitair Instituut voor Biotechnologie (VIB), Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussel, Belgium. joris.messens@vub.ac.be


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Arsenate reductase131Staphylococcus aureusMutation(s): 3 
Gene Names: ARSCSAP018
EC: 1.20.4.1
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: 1.70 Å
  • R-Value Free: 0.212 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.196 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 33.146α = 90
b = 34.377β = 90
c = 102.325γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
CNSrefinement

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-06-01
    Type: Initial release
  • Version 1.1: 2008-04-29
    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