Annotation

Description

The organic hydroperoxide resistance protein, thiol-dependent peroxidase that is a central player in response to stress induced by organic hydroperoxides in bacteria. It has unique three-dimensional structure and requires dithiols to support its activity. It forms an oval-shaped, tight homodimer and have two active site positioned on the opposite faces of the dimer. We have determined series of the structure of OHR-like protein from V. cholera and were able to reveal the enzymes structure in the reduce state (3I07), in the presence of captopril molecule (3LUS). FOX assays confirmed that it metabolizes hydrogen peroxide. 

Functional assignment

OHR 

Structure information

Unit cell parameters

Space Group

I 21 21 21  

Unit Cell

a=59.65Å, b=71.13Å, c=71.63Å
α=90.00, β=90.00, γ=90.00 

Solvent content

50.02  

Matthews coefficient

2.46  

Refinement

Data for the highest resolution shell is in parentheses.

Resolution range

40.00-1.45Å (1.49-1.45Å)  

R_all(%)

14.5 

R_work(%)

13.9 (21.5) 

R_free(%)

16.4 (27.1) 

Num. observed reflections

27216 (1820) 

Num. R_free reflections

1360 (103) 

Completeness(%)

99.0 (90.6) 

Model parameters

Num Atoms

1017  

Num Waters

182  

Num Hetatoms

236  

Model mean isotropic B factor

5.820Ų  

RMSD bond length

0.015Å  

RMSD bond angle

1.508°  

Filename uploaded

3EER.pdb (uploaded on Sep 16, 2009 5:03 PM)  

Inserted

Oct 27, 2008