1io3

From Proteopedia

(Difference between revisions)

Revision as of 06:03, 10 September 2015

CRYSTAL STRUCTURE OF FERRICYTOCHROME C2 FROM RHODOPSEUDOMONAS VIRIDIS

Structural highlights

1io3 is a 1 chain structure with sequence from Blastochloris viridis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1co6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CYC2_BLAVI] Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sogabe S, Miki K. Crystal structure of the oxidized cytochrome c(2) from Blastochloris viridis. FEBS Lett. 2001 Mar 2;491(3):174-9. PMID:11240122

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1io3"

Categories: Blastochloris viridis | Miki, K | Sogabe, S | Electron transport | Heme protein

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1co6|1co6]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1io3 RCSB], [http://www.ebi.ac.uk/pdbsum/1io3 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1io3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1io3 RCSB], [http://www.ebi.ac.uk/pdbsum/1io3 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CYC2_RHOVI CYC2_RHOVI]] Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria.
+[[http://www.uniprot.org/uniprot/CYC2_BLAVI CYC2_BLAVI]] Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1io3" style="background-color:#fffaf0;"></div>
 ==See Also==

1io3

From Proteopedia

Revision as of 06:03, 10 September 2015

CRYSTAL STRUCTURE OF FERRICYTOCHROME C2 FROM RHODOPSEUDOMONAS VIRIDIS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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