1rie

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[[Image:1rie.png|left|200px]]
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==STRUCTURE OF A WATER SOLUBLE FRAGMENT OF THE RIESKE IRON-SULFUR PROTEIN OF THE BOVINE HEART MITOCHONDRIAL CYTOCHROME BC1-COMPLEX==
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<StructureSection load='1rie' size='340' side='right' caption='[[1rie]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1rie]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RIE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RIE FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene><br>
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<tr><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>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rie OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1rie RCSB], [http://www.ebi.ac.uk/pdbsum/1rie PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ri/1rie_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BACKGROUND: The 'Rieske' iron-sulfur protein is the primary electron acceptor during hydroquinone oxidation in cytochrome bc complexes. The spectroscopic and electrochemical properties of the 'Rieske' [2Fe-2S] cluster differ significantly from those of other iron-sulfur clusters. A 129-residue water soluble fragment containing the intact [2Fe-2S] cluster was isolated following proteolytic digestion of the bc1 complex and used for structural studies. RESULTS: The structure of the Rieske iron-sulfur fragment containing the reduced [2Fe-2S] cluster has been determined using the multiwavelength anomalous diffraction (MAD) technique and refined at 1.5 A resolution. The fragment has a novel overall fold that includes three sheets of beta strands. The iron atoms of the [2Fe-2S] cluster are coordinated by two cysteine (Fe-1) and two histidine (Fe-2) residues, respectively, with the histidine ligands completely exposed to the solvent. This is in contrast to the four cysteine coordination pattern observed in previously characterised [2Fe-2S] ferredoxins. The cluster-binding fold is formed by two loops connected by a disulfide bridge; these loops superpose with the metal-binding loops of rubredoxins. The environment of the cluster is stabilised by an extensive hydrogen-bond network. CONCLUSIONS: The high-resolution structure supports the proposed coordination pattern involving histidine ligands and provides a basis for a detailed analysis of the spectroscopic and electrochemical properties. As the cluster is located at the tip of the protein, it might come into close contact with cytochrome b. The exposed N epsilon atoms of the histidine ligands of the cluster are readily accessible to quinones and inhibitors within the hydroquinone oxidation (QP) pocket of the bc1 complex and may undergo redox-dependent protonation/deprotonation.
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{{STRUCTURE_1rie| PDB=1rie | SCENE= }}
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Structure of a water soluble fragment of the 'Rieske' iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 A resolution.,Iwata S, Saynovits M, Link TA, Michel H Structure. 1996 May 15;4(5):567-79. PMID:8736555<ref>PMID:8736555</ref>
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===STRUCTURE OF A WATER SOLUBLE FRAGMENT OF THE RIESKE IRON-SULFUR PROTEIN OF THE BOVINE HEART MITOCHONDRIAL CYTOCHROME BC1-COMPLEX===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_8736555}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1rie]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RIE OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:008736555</ref><ref group="xtra">PMID:011880627</ref><ref group="xtra">PMID:014695246</ref><references group="xtra"/>
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Ubiquinol--cytochrome-c reductase]]
[[Category: Ubiquinol--cytochrome-c reductase]]

Revision as of 14:05, 29 September 2014

STRUCTURE OF A WATER SOLUBLE FRAGMENT OF THE RIESKE IRON-SULFUR PROTEIN OF THE BOVINE HEART MITOCHONDRIAL CYTOCHROME BC1-COMPLEX

1rie, resolution 1.50Å

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