2cb2

From Proteopedia

Revision as of 11:55, 30 October 2007

SULFUR OXYGENASE REDUCTASE FROM ACIDIANUS AMBIVALENS

Overview

Numerous microorganisms oxidize sulfur for energy conservation and, contribute to the global biogeochemical sulfur cycle. We have determined, the 1.7 angstrom-resolution structure of the sulfur oxygenase reductase, from the thermoacidophilic archaeon Acidianus ambivalens, which catalyzes, an oxygen-dependent disproportionation of elemental sulfur. Twenty-four, monomers form a large hollow sphere enclosing a positively charged, nanocompartment. Apolar channels provide access for linear sulfur species., A cysteine persulfide and a low-potential mononuclear non-heme iron site, ligated by a 2-His-1-carboxylate facial triad in a pocket of each subunit, constitute the active sites, accessible from the inside of the sphere. The, iron is likely the site of both sulfur oxidation and sulfur ... [(full description)]

About this Structure

2CB2 is a [Single protein] structure of sequence from [Acidianus ambivalens] with FE as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

X-ray Structure of a self-compartmentalizing sulfur cycle metalloenzyme., Urich T, Gomes CM, Kletzin A, Frazao C, Science. 2006 Feb 17;311(5763):996-1000. PMID:16484493

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