1qn2
CYTOCHROME CH FROM METHYLOBACTERIUM EXTORQUENS
OverviewOverview
Cytochrome cH is the electron donor to the oxidase in methylotrophic bacteria. Its amino acid sequence suggests that it is a typical Class 1 cytochrome c, but some features of the sequence indicated that its structure might be of special interest. The structure of oxidized cytochrome cH has been solved to 2.0 A resolution by X-ray diffraction. It has the classical tertiary structure of the Class 1 cytochromes c but bears a closer gross resemblance to mitochondrial cytochrome c than to the bacterial cytochrome c2. The left-hand side of the haem cleft is unique; in particular, it is highly hydrophobic, the usual water is absent, and the "conserved" Tyr67 is replaced by tryptophan. A number of features of the structure demonstrate that the usual hydrogen bonding network involving water in the haem channel is not essential and that other mechanisms may exist for modulation of redox potentials in this cytochrome.
About this StructureAbout this Structure
1QN2 is a Single protein structure of sequence from Methylobacterium extorquens. Full crystallographic information is available from OCA.
ReferenceReference
The molecular structure of an unusual cytochrome c2 determined at 2.0 A; the cytochrome cH from Methylobacterium extorquens., Read J, Gill R, Dales SL, Cooper JB, Wood SP, Anthony C, Protein Sci. 1999 Jun;8(6):1232-40. PMID:10386873 Page seeded by OCA on Sat May 3 06:28:19 2008