1JQK

Crystal structure of carbon monoxide dehydrogenase from Rhodospirillum rubrum

Summary for 1JQK

• Entry DOI: 10.2210/pdb1jqk/pdb
• Descriptor: carbon monoxide dehydrogenase, FE (II) ION, IRON/SULFUR CLUSTER, ... (5 entities in total)
• Functional Keywords: rossmann fold, oxidoreductase
• Biological source: Rhodospirillum rubrum
• Cellular location: Cytoplasm: P31896
• Total number of polymer chains: 6
• Total formula weight: 407194.57

Authors

Drennan, C.L.,Heo, J.,Sintchak, M.D.,Schreiter, E.,Ludden, P.W. (deposition date: 2001-08-07, release date: 2001-10-17, Last modification date: 2024-02-07)

Primary citation

Drennan, C.L.,Heo, J.,Sintchak, M.D.,Schreiter, E.,Ludden, P.W.
Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase.
Proc.Natl.Acad.Sci.USA, 98:11973-11978, 2001

PubMed Abstract: 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.

PubMed: 11593006
DOI: 10.1073/pnas.211429998

Experimental method

X-RAY DIFFRACTION (2.8 Å)