2num

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[[Image:2num.jpg|left|200px]]
 
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{{Structure
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==Soluble domain of Rieske Iron-Sulfur Protein==
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|PDB= 2num |SIZE=350|CAPTION= <scene name='initialview01'>2num</scene>, resolution 1.50&Aring;
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<StructureSection load='2num' size='340' side='right'caption='[[2num]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>
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<table><tr><td colspan='2'>[[2num]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NUM FirstGlance]. <br>
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|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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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|GENE= petA, fbcF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2num FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2num OCA], [https://pdbe.org/2num PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2num RCSB], [https://www.ebi.ac.uk/pdbsum/2num PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2num ProSAT]</span></td></tr>
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|RELATEDENTRY=[[2nuk|2NUK]], [[2nve|2NVE]], [[2nvf|2NVF]], [[2nvg|2NVG]], [[2nwf|2NWF]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2num FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2num OCA], [http://www.ebi.ac.uk/pdbsum/2num PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2num RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/UCRI_CERSP UCRI_CERSP] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
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== Evolutionary Conservation ==
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'''Soluble domain of Rieske Iron-Sulfur Protein'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nu/2num_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=2num 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 ==
The Rieske [2Fe-2S] iron-sulfur protein of cytochrome bc(1) functions as the initial electron acceptor in the rate-limiting step of the catalytic reaction. Prior studies have established roles for a number of conserved residues that hydrogen bond to ligands of the [2Fe-2S] cluster. We have constructed site-specific variants at two of these residues, measured their thermodynamic and functional properties, and determined atomic resolution X-ray crystal structures for the native protein at 1.2 A resolution and for five variants (Ser-154--&gt;Ala, Ser-154--&gt;Thr, Ser-154--&gt;Cys, Tyr-156--&gt;Phe, and Tyr-156--&gt;Trp) to resolutions between 1.5 A and 1.1 A. These structures and complementary biophysical data provide a molecular framework for understanding the role hydrogen bonds to the cluster play in tuning thermodynamic properties, and hence the rate of this bioenergetic reaction. These studies provide a detailed structure-function dissection of the role of hydrogen bonds in tuning the redox potentials of [2Fe-2S] clusters.
The Rieske [2Fe-2S] iron-sulfur protein of cytochrome bc(1) functions as the initial electron acceptor in the rate-limiting step of the catalytic reaction. Prior studies have established roles for a number of conserved residues that hydrogen bond to ligands of the [2Fe-2S] cluster. We have constructed site-specific variants at two of these residues, measured their thermodynamic and functional properties, and determined atomic resolution X-ray crystal structures for the native protein at 1.2 A resolution and for five variants (Ser-154--&gt;Ala, Ser-154--&gt;Thr, Ser-154--&gt;Cys, Tyr-156--&gt;Phe, and Tyr-156--&gt;Trp) to resolutions between 1.5 A and 1.1 A. These structures and complementary biophysical data provide a molecular framework for understanding the role hydrogen bonds to the cluster play in tuning thermodynamic properties, and hence the rate of this bioenergetic reaction. These studies provide a detailed structure-function dissection of the role of hydrogen bonds in tuning the redox potentials of [2Fe-2S] clusters.
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==About this Structure==
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Atomic resolution structures of rieske iron-sulfur protein: role of hydrogen bonds in tuning the redox potential of iron-sulfur clusters.,Kolling DJ, Brunzelle JS, Lhee S, Crofts AR, Nair SK Structure. 2007 Jan;15(1):29-38. PMID:17223530<ref>PMID:17223530</ref>
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2NUM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NUM OCA].
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==Reference==
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Atomic resolution structures of rieske iron-sulfur protein: role of hydrogen bonds in tuning the redox potential of iron-sulfur clusters., Kolling DJ, Brunzelle JS, Lhee S, Crofts AR, Nair SK, Structure. 2007 Jan;15(1):29-38. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17223530 17223530]
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[[Category: Rhodobacter sphaeroides]]
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[[Category: Single protein]]
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[[Category: Ubiquinol--cytochrome-c reductase]]
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[[Category: Brunzelle, J.]]
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[[Category: Crofts, A R.]]
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[[Category: Kolling, D.]]
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[[Category: Lhee, S.]]
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[[Category: Nair, S K.]]
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[[Category: iron sulfur cluster]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:08:39 2008''
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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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<div class="pdbe-citations 2num" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Cereibacter sphaeroides]]
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[[Category: Large Structures]]
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[[Category: Brunzelle J]]
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[[Category: Crofts AR]]
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[[Category: Kolling D]]
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[[Category: Lhee S]]
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[[Category: Nair SK]]

Current revision

Soluble domain of Rieske Iron-Sulfur Protein

PDB ID 2num

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