1IO3

CRYSTAL STRUCTURE OF FERRICYTOCHROME C2 FROM RHODOPSEUDOMONAS VIRIDIS

Summary for 1IO3

• Entry DOI: 10.2210/pdb1io3/pdb
• Related: 1co6
• Descriptor: CYTOCHROME C2, HEME C (3 entities in total)
• Functional Keywords: heme protein, electron transport
• Biological source: Blastochloris viridis
• Total number of polymer chains: 1
• Total formula weight: 12285.72

Authors

Miki, K.,Sogabe, S. (deposition date: 2001-01-06, release date: 2001-04-18, Last modification date: 2024-10-23)

Primary citation

Sogabe, S.,Miki, K.
Crystal structure of the oxidized cytochrome c(2) from Blastochloris viridis.
FEBS Lett., 491:174-179, 2001

PubMed Abstract: 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.

PubMed: 11240122
DOI: 10.1016/S0014-5793(01)02179-2

Experimental method

X-RAY DIFFRACTION (1.9 Å)