1io3: Difference between revisions
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|PDB= 1io3 |SIZE=350|CAPTION= <scene name='initialview01'>1io3</scene>, resolution 1.9Å | |PDB= 1io3 |SIZE=350|CAPTION= <scene name='initialview01'>1io3</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1co6|1co6]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1io3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1io3 OCA], [http://www.ebi.ac.uk/pdbsum/1io3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1io3 RCSB]</span> | |||
}} | }} | ||
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[[Category: Miki, K.]] | [[Category: Miki, K.]] | ||
[[Category: Sogabe, S.]] | [[Category: Sogabe, S.]] | ||
[[Category: heme protein]] | [[Category: heme protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:22:19 2008'' | ||
Revision as of 21:22, 30 March 2008
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| , resolution 1.9Å | |||||||
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| Related: | 1co6
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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