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PDBsum entry 1z2d

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protein links
Oxidoreductase PDB id
1z2d
Jmol
Contents
Protein chain
139 a.a. *
* Residue conservation analysis
PDB id:
1z2d
Name: Oxidoreductase
Title: Solution structure of bacillus subtilis arsc in reduced state
Structure: Arsenate reductase. Chain: a. Synonym: arsenical pump modifier. Engineered: yes
Source: Bacillus subtilis. Organism_taxid: 1423. Expressed in: escherichia coli. Expression_system_taxid: 562
NMR struc: 20 models
Authors: C.Jin,Y.Li
Key ref:
X.Guo et al. (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. PubMed id: 16192272 DOI: 10.1074/jbc.M508132200
Date:
08-Mar-05     Release date:   04-Oct-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P45947  (ARSC_BACSU) -  Protein ArsC
Seq:
Struc:
139 a.a.
139 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 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
+ 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: 10.1074/jbc.M508132200 J Biol Chem 280:39601-39608 (2005)
PubMed id: 16192272  
 
 
Solution structures and backbone dynamics of arsenate reductase from Bacillus subtilis: reversible conformational switch associated with arsenate reduction.
X.Guo, Y.Li, K.Peng, Y.Hu, C.Li, B.Xia, C.Jin.
 
  ABSTRACT  
 
Arsenate reductase encoded by the chromosomal arsC gene in Bacillus subtilis catalyzes the intracellular reduction of arsenate to arsenite, which is then extruded from cells through an efficient and specific transport system. Herein, we present the solution structures and backbone dynamics of both the reduced and oxidized forms of arsenate reductase from B. subtilis. The overall structures of both forms are similar to those of bovine low molecular weight protein-tyrosine phosphatase and arsenate reductase from Staphylococcus aureus. However, several features of the tertiary structure and mobility are notably different between the reduced and oxidized forms of B. subtilis arsenate reductase, particularly in the P-loop region and the segment Cys(82)-Cys(89). The backbone dynamics results demonstrated that the reduced form of arsenate reductase undergoes millisecond conformational changes in the functional P-loop and Cys(82)-Cys(89), which may facilitate the formation of covalent intermediates and subsequent reduction of arsenate. In the oxidized form, Cys(82)-Cys(89) shows motional flexibility on both picosecond-to-nanosecond and possibly millisecond time scales, which may facilitate the reduction of the oxidized enzyme by thioredoxin to regenerate the active enzyme. Overall, the internal dynamics and static structures of the enzyme provide insights into the molecular mechanism of arsenate reduction, especially the reversible conformational switch and changes in internal motions associated with the catalytic reaction.
 
  Selected figure(s)  
 
Figure 3.
FIGURE 3. Structural comparison. A, overlay of the C^ trace of the solution structures of the reduced (red) and oxidized (green) forms of B. subtilis ArsC; B, comparison of the local structures of the P-loop of the reduced (left) and oxidized (right) forms of ArsC; C, the C^ trace of reduced B. subtilis ArsC in solution (red) superimposed with chain A of the crystal structure (blue); D, the C^ trace of reduced B. subtilis ArsC (red) superimposed with that of bovine low molecular weight protein-tyrosine phosphatase (magenta); E, the C^ trace of reduced B. subtilis ArsC (red) superimposed with that of S. aureus ArsC (cyan); F, the C^ trace of oxidized B. subtilis ArsC (green) superimposed with that of S. aureus ArsC (yellow).
Figure 5.
FIGURE 5. Ribbon diagrams representing the dynamic properties of B. subtilis ArsC. The ribbon diagrams of the reduced (A) and oxidized (B) forms of B. subtilis ArsC represent the internal motions on picosecond-to-nanosecond time scales, with colors ranging from yellow to red and magenta corresponding to [e] values from 10 to 100 ps and >100 ps, respectively. The ribbon diagrams of the reduced (C) and oxidized (D) forms of B. subtilis ArsC represent the residues with conformational changes (R[ex] > 1 s-1) on the millisecond time scale, colored in blue.
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2005, 280, 39601-39608) copyright 2005.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
  19902501 G.Roos, P.Geerlings, and J.Messens (2010).
The conserved active site tryptophan of thioredoxin has no effect on its redox properties.
  Protein Sci, 19, 190-194.  
19675666 G.Roos, N.Foloppe, K.Van Laer, L.Wyns, L.Nilsson, P.Geerlings, and J.Messens (2009).
How thioredoxin dissociates its mixed disulfide.
  PLoS Comput Biol, 5, e1000461.  
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.  
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.