2c8s
From Proteopedia
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CYTOCHROME CL FROM METHYLOBACTERIUM EXTORQUENS
Overview
The structure of cytochrome cL from Methylobacterium extorquens has been, determined by X-ray crystallography to a resolution of 1.6 A. This, unusually large, acidic cytochrome is the physiological electron acceptor, for the quinoprotein methanol dehydrogenase in the periplasm of, methylotrophic bacteria. Its amino acid sequence is completely different, from that of other cytochromes but its X-ray structure reveals a core that, is typical of class I cytochromes c, having alpha-helices folded into a, compact structure enclosing the single haem c prosthetic group and leaving, one edge of the haem exposed. The haem is bound through thioether bonds to, Cys65 and Cys68, and the fifth ligand to the haem iron is provided by, His69. Remarkably, the sixth ligand is provided by His112, and not by, ... [(full description)]
About this Structure
2C8S is a [Single protein] structure of sequence from [Methylobacterium extorquens] with CA and HEM as [ligands]. This structure superseeds the now removed PDB entry 1UMM. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
The 1.6A X-ray structure of the unusual c-type cytochrome, cytochrome cL, from the methylotrophic bacterium Methylobacterium extorquens., Williams P, Coates L, Mohammed F, Gill R, Erskine P, Bourgeois D, Wood SP, Anthony C, Cooper JB, J Mol Biol. 2006 Mar 17;357(1):151-62. Epub 2006 Jan 5. PMID:16414073
Page seeded by OCA on Tue Oct 30 17:01:41 2007
Categories: Methylobacterium extorquens | Single protein | Anthony, C. | Coates, L. | Cooper, J.B. | Erskine, P. | Gill, R. | Mohammed, F. | Williams, P.A. | Wood, S.P. | CA | HEM | Cytochrome c | Electron transport | Haem | Heme | Metal-binding
