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2lit

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Revision as of 23:26, 24 December 2014

NMR Solution Structure of Yeast Iso-1-cytochrome c Mutant P71H in reduced states

Structural highlights

2lit is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2lir
Gene:	CYC1, YJR048W, J1653 (Saccharomyces cerevisiae)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[CYC1_YEAST] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.

Publication Abstract from PubMed

To convert cyt c into a peroxidase-like metalloenzyme, the P71H mutant was designed to introduce a distal histidine. Unexpectedly, its peroxidase activity was found even lower than that of the native, and that the axial ligation of heme iron was changed to His71/His18 in the oxidized state, while to Met80/His18 in the reduced state, characterized by UV-visible, circular dichroism, and resonance Raman spectroscopy. To further probe the functional importance of Pro71 in oxidation state dependent conformational changes occurred in cyt c, the solution structures of P71H mutant in both oxidation states were determined. The structures indicate that the half molecule of cyt c (aa 50-102) presents a kind of "zigzag riveting ruler" structure, residues at certain positions of this region such as Pro71, Lys73 can move a big distance by altering the tertiary structure while maintaining the secondary structures. This finding provides a molecular insight into conformational toggling in different oxidation states of cyt c that is principle significance to its biological functions in electron transfer and apoptosis. Structural analysis also reveals that Pro71 functions as a key hydrophobic patch in the folding of the polypeptide of the region (aa 50-102), to prevent heme pocket from the solvent.

Conformational toggling of yeast iso-1-cytochrome C in the oxidized and reduced States.,Lan W, Wang Z, Yang Z, Zhu J, Ying T, Jiang X, Zhang X, Wu H, Liu M, Tan X, Cao C, Huang ZX PLoS One. 2011;6(11):e27219. Epub 2011 Nov 8. PMID:22087268^[1]

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

References

↑ Lan W, Wang Z, Yang Z, Zhu J, Ying T, Jiang X, Zhang X, Wu H, Liu M, Tan X, Cao C, Huang ZX. Conformational toggling of yeast iso-1-cytochrome C in the oxidized and reduced States. PLoS One. 2011;6(11):e27219. Epub 2011 Nov 8. PMID:22087268 doi:10.1371/journal.pone.0027219

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2lit"

@@ Line 8: / Line 8: @@
 <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=2lit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lit OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lit RCSB], [http://www.ebi.ac.uk/pdbsum/2lit PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/CYC1_YEAST CYC1_YEAST]] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2lit

From Proteopedia

Revision as of 23:26, 24 December 2014

NMR Solution Structure of Yeast Iso-1-cytochrome c Mutant P71H in reduced states

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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