spacer
spacer

PDBsum entry 1rxe

Go to PDB code: 
protein ligands metals links
Oxidoreductase PDB id
1rxe
Jmol
Contents
Protein chain
131 a.a. *
Ligands
LCP
MNB
Metals
__K
Waters ×125
* Residue conservation analysis
PDB id:
1rxe
Name: Oxidoreductase
Title: Arsc complexed with mnb
Structure: Arsenate reductase. Chain: a. Synonym: arsc, arsenical pump modifier. Engineered: yes. Mutation: yes
Source: Staphylococcus aureus. Organism_taxid: 1280. Gene: arsc, sap018. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.70Å     R-factor:   0.195     R-free:   0.212
Authors: J.Messens,I.Van Molle,P.Vanhaesebrouck,M.Limbourg,K.Van Belle,K.Wahni,J.C.Martins,R.Loris,L.Wyns
Key ref:
J.Messens et al. (2004). The structure of a triple mutant of pI258 arsenate reductase from Staphylococcus aureus and its 5-thio-2-nitrobenzoic acid adduct. Acta Crystallogr D Biol Crystallogr, 60, 1180-1184. PubMed id: 15159594 DOI: 10.1107/S0907444904007334
Date:
18-Dec-03     Release date:   01-Jun-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0A006  (ARSC_STAAU) -  Protein ArsC
Seq:
Struc:
131 a.a.
131 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.1.3.48  - Protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Protein tyrosine phosphate
+ H(2)O
=
protein tyrosine
Bound ligand (Het Group name = MNB)
matches with 42.00% similarity
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     peptidyl-tyrosine dephosphorylation   4 terms 
  Biochemical function     oxidoreductase activity     4 terms  

 

 
    reference    
 
 
DOI no: 10.1107/S0907444904007334 Acta Crystallogr D Biol Crystallogr 60:1180-1184 (2004)
PubMed id: 15159594  
 
 
The structure of a triple mutant of pI258 arsenate reductase from Staphylococcus aureus and its 5-thio-2-nitrobenzoic acid adduct.
J.Messens, I.Van Molle, P.Vanhaesebrouck, K.Van Belle, K.Wahni, J.C.Martins, L.Wyns, R.Loris.
 
  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.
 
  Selected figure(s)  
 
Figure 1.
Figure 1 (a) The structure of wild-type ArsC in the reduced state (PDB code [38]1ljl ). The short redox helix bearing Cys82 and Cys89 (green) is structured. (b) The structure of ArsC C15A in the oxidized state (PDB code [39]1lju ). The short redox helix is looped-out (green). In this structure, arsenite is bound in the active site P-loop. In both structures, the redox-active cysteines (in stick representation) and the P-loop active site (red) are shown. The figures were prepared using the program PyMol 0.9 (DeLano Scientific).
Figure 4.
Figure 4 (a) F[o] - F[c] omit electron-density map of 5-thio-2-nitrobenzoate (TNB) bound to Cys89 in the structure of C10SC15AC82S (PDB code [117]1rxe ) at 1.7 . The map is contoured at 3.0 [118][sigma] . Figure prepared using the program MOLSCRIPT (Kraulis, 1991[119] [Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.]-[120][bluearr.gif] ). (b) The TNB molecule as observed in its structural hydrophobic environment. The figure was prepared using PyMol 0.9 (DeLano Scientific).
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2004, 60, 1180-1184) copyright 2004.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21258851 S.Jain, B.Saluja, A.Gupta, S.S.Marla, and R.Goel (2011).
Validation of Arsenic Resistance in Bacillus cereus Strain AG27 by Comparative Protein Modeling of arsC Gene Product.
  Protein J, 30, 91.  
19304854 L.López-Maury, A.M.Sánchez-Riego, J.C.Reyes, and F.J.Florencio (2009).
The glutathione/glutaredoxin system is essential for arsenate reduction in Synechocystis sp. strain PCC 6803.
  J Bacteriol, 191, 3534-3543.  
17303556 Y.Li, Y.Hu, X.Zhang, H.Xu, E.Lescop, B.Xia, and C.Jin (2007).
Conformational fluctuations coupled to the thiol-disulfide transfer between thioredoxin and arsenate reductase in Bacillus subtilis.
  J Biol Chem, 282, 11078-11083.
PDB codes: 2gzy 2gzz 2ipa
16133099 S.Silver, and l.e. .T.Phung (2005).
A bacterial view of the periodic table: genes and proteins for toxic inorganic ions.
  J Ind Microbiol Biotechnol, 32, 587-605.  
16192272 X.Guo, Y.Li, K.Peng, Y.Hu, C.Li, B.Xia, and C.Jin (2005).
Solution structures and backbone dynamics of arsenate reductase from Bacillus subtilis: reversible conformational switch associated with arsenate reduction.
  J Biol Chem, 280, 39601-39608.
PDB codes: 1z2d 1z2e
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.