2num: Difference between revisions

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-{{Seed}}
-[[Image:2num.png|left|200px]]
-<!--
+==Soluble domain of Rieske Iron-Sulfur Protein==
-The line below this paragraph, containing "STRUCTURE_2num", creates the "Structure Box" on the page.
+<StructureSection load='2num' size='340' side='right'caption='[[2num]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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>
--->
+<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>
-{{STRUCTURE_2num|  PDB=2num  |  SCENE=  }}
+<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>
+</table>
+== Function ==
+[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.
+== 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/nu/2num_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=2num ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-===Soluble domain of Rieske Iron-Sulfur Protein===
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_17223530}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2num" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 17223530 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17223530}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Cereibacter sphaeroides]]
-NUM 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].
+[[Category: Large Structures]]
+[[Category: Brunzelle J]]
-==Reference==
+[[Category: Crofts AR]]
-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]
+[[Category: Kolling D]]
-[[Category: Rhodobacter sphaeroides]]
+[[Category: Lhee S]]
-[[Category: Single protein]]
+[[Category: Nair SK]]
-[[Category: Ubiquinol--cytochrome-c reductase]]
-[[Category: Brunzelle, J.]]
-[[Category: Crofts, A R.]]
-[[Category: Kolling, D.]]
-[[Category: Lhee, S.]]
-[[Category: Nair, S K.]]
-[[Category: Iron sulfur cluster]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:34:05 2008''