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3cx5
From Proteopedia
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| - | + | ==Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer.== | |
| - | + | <StructureSection load='3cx5' size='340' side='right' caption='[[3cx5]], [[Resolution|resolution]] 1.90Å' scene=''> | |
| - | {{ | + | == Structural highlights == |
| + | <table><tr><td colspan='2'>[[3cx5]] is a 23 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CX5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CX5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6PH:(1R)-2-(PHOSPHONOOXY)-1-[(TRIDECANOYLOXY)METHYL]ETHYL+PENTADECANOATE'>6PH</scene>, <scene name='pdbligand=7PH:(1R)-2-(DODECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL+TETRADECANOATE'>7PH</scene>, <scene name='pdbligand=8PE:(2R)-3-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-2-(TETRADECANOYLOXY)PROPYL+OCTADECANOATE'>8PE</scene>, <scene name='pdbligand=9PE:(1R)-2-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(HEPTANOYLOXY)METHYL]ETHYL+OCTADECANOATE'>9PE</scene>, <scene name='pdbligand=CN3:(2R,5S,11R,14R)-5,8,11-TRIHYDROXY-2-(NONANOYLOXY)-5,11-DIOXIDO-16-OXO-14-[(PROPANOYLOXY)METHYL]-4,6,10,12,15-PENTAOXA-5,11-DIPHOSPHANONADEC-1-YL+UNDECANOATE'>CN3</scene>, <scene name='pdbligand=CN5:(5S,11R)-5,8,11-TRIHYDROXY-5,11-DIOXIDO-17-OXO-4,6,10,12,16-PENTAOXA-5,11-DIPHOSPHAOCTADEC-1-YL+PENTADECANOATE'>CN5</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SMA:STIGMATELLIN+A'>SMA</scene>, <scene name='pdbligand=SUC:SUCROSE'>SUC</scene>, <scene name='pdbligand=UMQ:UNDECYL-MALTOSIDE'>UMQ</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3cxh|3cxh]], [[1ezv|1ezv]], [[1kb9|1kb9]], [[1kyo|1kyo]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquinol--cytochrome-c_reductase Ubiquinol--cytochrome-c reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.2.2 1.10.2.2] </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=3cx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cx5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cx5 RCSB], [http://www.ebi.ac.uk/pdbsum/3cx5 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cx/3cx5_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In cellular respiration, cytochrome c transfers electrons from cytochrome bc(1) complex (complex III) to cytochrome c oxidase by transiently binding to the membrane proteins. Here, we report the structure of isoform-1 cytochrome c bound to cytochrome bc(1) complex at 1.9 A resolution in reduced state. The dimer structure is asymmetric. Monovalent cytochrome c binding is correlated with conformational changes of the Rieske head domain and subunit QCR6p and with a higher number of interfacial water molecules bound to cytochrome c(1). Pronounced hydration and a "mobility mismatch" at the interface with disordered charged residues on the cytochrome c side are favorable for transient binding. Within the hydrophobic interface, a minimal core was identified by comparison with the novel structure of the complex with bound isoform-2 cytochrome c. Four core interactions encircle the heme cofactors surrounded by variable interactions. The core interface may be a feature to gain specificity for formation of the reactive complex. | ||
| - | + | Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer.,Solmaz SR, Hunte C J Biol Chem. 2008 Jun 20;283(25):17542-9. Epub 2008 Apr 4. PMID:18390544<ref>PMID:18390544</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
==See Also== | ==See Also== | ||
*[[Cytochrome bc1 complex|Cytochrome bc1 complex]] | *[[Cytochrome bc1 complex|Cytochrome bc1 complex]] | ||
*[[Cytochrome c|Cytochrome c]] | *[[Cytochrome c|Cytochrome c]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Ubiquinol--cytochrome-c reductase]] | [[Category: Ubiquinol--cytochrome-c reductase]] | ||
| - | [[Category: Hunte, C | + | [[Category: Hunte, C]] |
| - | [[Category: Solmaz, S R.N | + | [[Category: Solmaz, S R.N]] |
[[Category: Complex iii]] | [[Category: Complex iii]] | ||
[[Category: Cytochrome bc1 complex]] | [[Category: Cytochrome bc1 complex]] | ||
Revision as of 13:55, 18 December 2014
Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer.
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Categories: Mus musculus | Saccharomyces cerevisiae | Ubiquinol--cytochrome-c reductase | Hunte, C | Solmaz, S R.N | Complex iii | Cytochrome bc1 complex | Cytochrome c | Electron transfer complex | Electron transport | Heme | Inner membrane | Iron | Iron-sulfur | Metal-binding | Methylation | Mitochondrialtransmembrane complex | Mitochondrion | Oxidoreductase | Phosphoprotein | Respiratory chain | Transient protein-protein interaction | Transit peptide | Transport

