1jqk

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1jqk, resolution 2.8Å

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Crystal structure of carbon monoxide dehydrogenase from Rhodospirillum rubrum

Overview

A crystal structure of the anaerobic Ni-Fe-S carbon monoxide dehydrogenase, (CODH) from Rhodospirillum rubrum has been determined to 2.8-A resolution., The CODH family, for which the R. rubrum enzyme is the prototype, catalyzes the biological oxidation of CO at an unusual Ni-Fe-S cluster, called the C-cluster. The Ni-Fe-S C-cluster contains a mononuclear site, and a four-metal cubane. Surprisingly, anomalous dispersion data suggest, that the mononuclear site contains Fe and not Ni, and the four-metal, cubane has the form [NiFe(3)S(4)] and not [Fe(4)S(4)]. The mononuclear, site and the four-metal cluster are bridged by means of Cys(531) and one, of the sulfides of the cube. CODH is organized as a dimer with a, previously unidentified [Fe(4)S(4)] cluster bridging the two subunits., Each monomer is comprised of three domains: a helical domain at the N, terminus, an alpha/beta (Rossmann-like) domain in the middle, and an, alpha/beta (Rossmann-like) domain at the C terminus. The helical domain, contributes ligands to the bridging [Fe(4)S(4)] cluster and another, [Fe(4)S(4)] cluster, the B-cluster, which is involved in electron, transfer. The two Rossmann domains contribute ligands to the active site, C-cluster. This x-ray structure provides insight into the mechanism of, biological CO oxidation and has broader significance for the roles of Ni, and Fe in biological systems.

About this Structure

1JQK is a Single protein structure of sequence from Rhodospirillum rubrum with FE2, SF4, WCC and UNX as ligands. Active as Carbon-monoxide dehydrogenase (acceptor), with EC number 1.2.99.2 Full crystallographic information is available from OCA.

Reference

Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase., Drennan CL, Heo J, Sintchak MD, Schreiter E, Ludden PW, Proc Natl Acad Sci U S A. 2001 Oct 9;98(21):11973-8. Epub 2001 Oct 2. PMID:11593006

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