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Structure of IDP01300

Arsenate reductase from Vibrio cholerae

Edit deposit information
CSGID target
IDP01300 
PDB Id
3F0I (NCBI MMDB
Authors
J.Osipiuk,M.Gu,J.Stam,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Jerzy Osipiuk 
Responsible lab
Argonne National Laboratory 
Deposition Date
Oct 24, 2008 
Release Date
Nov 11, 2008 

Annotation

Description
The ubiquity of arsenic in the environment has led to the evolution of enzymes for arsenic detoxification. An initial step in arsenic metabolism is the enzymatic reduction of arsenate [As(V)] to arsenite [As(III)] which could be catalyzed in bacteria by arsenate reductases (ArsC) which are members of the Thioredoxin-like protein family. ArsC proteins from different sources have unrelated sequences and structural folds. Arsenate reductase is unusual among well-studied enzyme classes due to the diversity of several independent enzyme families. ArsC from Vibrio cholerae is similar to that encoded by ArsC on the R733 plasmid of Escherichia coli. The purified enzyme exhibits arsenate reductase activity dependent on the presence of reduced glutathione (GSH) and glutaredoxin (Grx). The enzyme uses three separate cysteine residues as it was observed for the thioredoxin-linked enzymes. However, in case of ArsC protein, only one cysteine residue is in the arsenate reductase primary enzyme sequence and the others occur in GSH and Grx.  
Functional assignment
 

Ligands

Ligand code Name Ligand type
MLI
NA Sodium ion
MSE modified residue

Structure information

Unit cell parameters

Space Group
P 64 2 2  
Unit Cell

a=118.70Å, b=118.70Å, c=110.01Å
α=90.00, β=90.00, γ=120.00 
Solvent content
69.98  
Matthews coefficient
4.1  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
31.80-1.88Å (1.93-1.88Å)  
Rall(%)
16.7 
Rwork(%)
16.6 (23.9) 
Rfree(%)
18.9 (28.5) 
Num. observed reflections
37124 (2715) 
Num. Rfree reflections
1856 (153) 
Completeness(%)
98.5 (99.6) 

Model parameters

Num Atoms
2266  
Num Waters
301  
Num Hetatoms
0  
Model mean isotropic B factor
16.942Å2  
RMSD bond length
0.018Å  
RMSD bond angle
1.534°  
Filename uploaded
idp01300.pdb (uploaded on Oct 28, 2008 10:31 AM)  
Inserted
Oct 28, 2008