1io3
From Proteopedia
(New page: 200px<br /><applet load="1io3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1io3, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1io3.jpg|left|200px]]<br /><applet load="1io3" size=" | + | [[Image:1io3.jpg|left|200px]]<br /><applet load="1io3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1io3, resolution 1.9Å" /> | caption="1io3, resolution 1.9Å" /> | ||
'''CRYSTAL STRUCTURE OF FERRICYTOCHROME C2 FROM RHODOPSEUDOMONAS VIRIDIS'''<br /> | '''CRYSTAL STRUCTURE OF FERRICYTOCHROME C2 FROM RHODOPSEUDOMONAS VIRIDIS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the oxidized cytochrome c(2) from Blastochloris | + | 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 Structure== | ==About this Structure== | ||
| - | 1IO3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Blastochloris_viridis Blastochloris viridis] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1IO3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Blastochloris_viridis Blastochloris viridis] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IO3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: heme protein]] | [[Category: heme protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:48 2008'' |
Revision as of 11:13, 21 February 2008
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CRYSTAL STRUCTURE OF FERRICYTOCHROME C2 FROM RHODOPSEUDOMONAS VIRIDIS
Overview
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 Structure
1IO3 is a Single protein structure of sequence from Blastochloris viridis with as ligand. Full crystallographic information is available from OCA.
Reference
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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