1io3
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CRYSTAL STRUCTURE OF FERRICYTOCHROME C2 FROM RHODOPSEUDOMONAS VIRIDIS
OverviewOverview
The crystal structure of the oxidized cytochrome c(2) from Blastochloris, (formerly Rhodopseudomonas) viridis was determined at 1.9 A resolution., Structural comparison with the reduced form revealed significant, structural changes according to the oxidation state of the heme iron., Slight perturbation of the polypeptide chain backbone was observed, and, the secondary structure and the hydrogen patterns between main-chain atoms, were retained. The oxidation state-dependent conformational shifts were, localized in the vicinity of the methionine ligand side and the propionate, group of the heme. The conserved segment of the polypeptide chain in, cytochrome c and cytochrome c(2) exhibited some degree of mobility, interacting with the heme iron atom by the hydrogen bond network. These, results indicate that the movement of the internal water molecule, conserved in various c-type cytochromes drives the adjustments of, side-chain atoms of nearby residue, and the segmental temperature factor, changes along the polypeptide chain.
About this StructureAbout this Structure
1IO3 is a Single protein structure of sequence from Blastochloris viridis with HEM as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the oxidized cytochrome c(2) from Blastochloris viridis., Sogabe S, Miki K, FEBS Lett. 2001 Mar 2;491(3):174-9. PMID:11240122
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