2fyu: Difference between revisions

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-[[Image:2fyu.gif|left|200px]]
- {{Structure
+==Crystal structure of bovine heart mitochondrial bc1 with jg144 inhibitor==
-|PDB= 2fyu |SIZE=350|CAPTION= <scene name='initialview01'>2fyu</scene>, resolution 2.26&Aring;
+<StructureSection load='2fyu' size='340' side='right'caption='[[2fyu]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=FDN:(5S)-3-ANILINO-5-(2,4-DIFLUOROPHENYL)-5-METHYL-1,3-OXAZOLIDINE-2,4-DIONE'>FDN</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>
+<table><tr><td colspan='2'>[[2fyu]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FYU FirstGlance]. <br>
-|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FDN:(5S)-3-ANILINO-5-(2,4-DIFLUOROPHENYL)-5-METHYL-1,3-OXAZOLIDINE-2,4-DIONE'>FDN</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fyu OCA], [https://pdbe.org/2fyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fyu RCSB], [https://www.ebi.ac.uk/pdbsum/2fyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fyu ProSAT]</span></td></tr>
-|RELATEDENTRY=[[1qcr|1QCR]], [[1l0n|1L0N]], [[1l0l|1L0L]], [[1sqx|1SQX]], [[1sqv|1SQV]]
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fyu OCA], [http://www.ebi.ac.uk/pdbsum/2fyu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fyu RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/QCR1_BOVIN QCR1_BOVIN] This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1.
+== 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/fy/2fyu_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=2fyu ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+In the cytochrome bc(1) complex, the swivel motion of the iron-sulfur protein (ISP) between two redox sites constitutes a key component of the mechanism that achieves the separation of the two electrons in a substrate molecule at the quinol oxidation (Q(o)) site. The question remaining is how the motion of ISP is controlled so that only one electron enters the thermodynamically favorable chain via ISP. An analysis of eight structures of mitochondrial bc(1) with bound Q(o) site inhibitors revealed that the presence of inhibitors causes a bidirectional repositioning of the cd1 helix in the cytochrome b subunit. As the cd1 helix forms a major part of the ISP binding crater, any positional shift of this helix modulates the ability of cytochrome b to bind ISP. The analysis also suggests a mechanism for reversal of the ISP fixation when the shape complementarity is significantly reduced after a positional reorientation of the reaction product quinone. The importance of shape complementarity in this mechanism was confirmed by functional studies of bc(1) mutants and by a structure determination of the bacterial form of bc(1). A mechanism for the high fidelity of the bifurcated electron transfer is proposed.
-'''Crystal structure of bovine heart mitochondrial bc1 with jg144 inhibitor'''
+Surface-modulated motion switch: capture and release of iron-sulfur protein in the cytochrome bc1 complex.,Esser L, Gong X, Yang S, Yu L, Yu CA, Xia D Proc Natl Acad Sci U S A. 2006 Aug 29;103(35):13045-50. Epub 2006 Aug 21. PMID:16924113<ref>PMID:16924113</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2fyu" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-In the cytochrome bc(1) complex, the swivel motion of the iron-sulfur protein (ISP) between two redox sites constitutes a key component of the mechanism that achieves the separation of the two electrons in a substrate molecule at the quinol oxidation (Q(o)) site. The question remaining is how the motion of ISP is controlled so that only one electron enters the thermodynamically favorable chain via ISP. An analysis of eight structures of mitochondrial bc(1) with bound Q(o) site inhibitors revealed that the presence of inhibitors causes a bidirectional repositioning of the cd1 helix in the cytochrome b subunit. As the cd1 helix forms a major part of the ISP binding crater, any positional shift of this helix modulates the ability of cytochrome b to bind ISP. The analysis also suggests a mechanism for reversal of the ISP fixation when the shape complementarity is significantly reduced after a positional reorientation of the reaction product quinone. The importance of shape complementarity in this mechanism was confirmed by functional studies of bc(1) mutants and by a structure determination of the bacterial form of bc(1). A mechanism for the high fidelity of the bifurcated electron transfer is proposed.
+*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
+*[[Cytochrome bc1 3D structures|Cytochrome bc1 3D structures]]
-==About this Structure==
+== References ==
-FYU is a [[Protein complex]] structure of sequences 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=2FYU OCA].
+<references/>
+__TOC__
-==Reference==
+</StructureSection>
-Surface-modulated motion switch: capture and release of iron-sulfur protein in the cytochrome bc1 complex., Esser L, Gong X, Yang S, Yu L, Yu CA, Xia D, Proc Natl Acad Sci U S A. 2006 Aug 29;103(35):13045-50. Epub 2006 Aug 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16924113 16924113]
 [[Category: Bos taurus]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Ubiquinol--cytochrome-c reductase]]
+[[Category: Esser L]]
-[[Category: Esser, L.]]
+[[Category: Xia D]]
-[[Category: Xia, D.]]
-[[Category: 11 protein complex]]
-[[Category: transmembrane helice]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:09:32 2008''