2q62

From Proteopedia

(Difference between revisions)
Jump to: navigation, search

OCA (Talk | contribs)
(New page: 200px<br /><applet load="2q62" size="350" color="white" frame="true" align="right" spinBox="true" caption="2q62, resolution 1.800&Aring;" /> '''Crystal Structure o...)
Next diff →

Revision as of 09:44, 23 January 2008


2q62, resolution 1.800Å

Drag the structure with the mouse to rotate

Crystal Structure of ArsH from Sinorhizobium meliloti

Overview

Purified ArsH from Sinorhizobium meliloti exhibits NADPH:FMN-dependent, reduction of molecular O2 to hydrogen peroxide and catalyzes reduction of, azo dyes. The structure of ArsH was determined at 1.8A resolution. ArsH, crystallizes with eight molecules in the asymmetric unit forming two, tetramers. Each monomer has a core domain with a central five-stranded, parallel beta-sheet and two monomers interact to form a classical, flavodoxin-like dimer. The N- and C-terminal extensions of ArsH are, involved in interactions between subunits and tetramer formation. The, structure may provide insight in how ArsH participates in arsenic, detoxification.

About this Structure

2Q62 is a Single protein structure of sequence from Sinorhizobium meliloti with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti., Ye J, Yang HC, Rosen BP, Bhattacharjee H, FEBS Lett. 2007 Aug 21;581(21):3996-4000. Epub 2007 Jul 25. PMID:17673204

Page seeded by OCA on Wed Jan 23 11:44:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools