1io3: Difference between revisions

Revision as of 13:39, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1io3.png

Template:STRUCTURE 1io3

CRYSTAL STRUCTURE OF FERRICYTOCHROME C2 FROM RHODOPSEUDOMONAS VIRIDISCRYSTAL STRUCTURE OF FERRICYTOCHROME C2 FROM RHODOPSEUDOMONAS VIRIDIS

Template:ABSTRACT PUBMED 11240122

About this StructureAbout this Structure

1IO3 is a Single protein structure of sequence from Blastochloris viridis. 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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-'''CRYSTAL STRUCTURE OF FERRICYTOCHROME C2 FROM RHODOPSEUDOMONAS VIRIDIS'''
+===CRYSTAL STRUCTURE OF FERRICYTOCHROME C2 FROM RHODOPSEUDOMONAS VIRIDIS===
-==Overview==
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-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.
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 [[Category: Sogabe, S.]]
 [[Category: Heme protein]]
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