2fwl: Difference between revisions

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-{{Seed}}
-[[Image:2fwl.png|left|200px]]
-<!--
+==The cytochrome c552/CuA complex from Thermus thermophilus==
-The line below this paragraph, containing "STRUCTURE_2fwl", creates the "Structure Box" on the page.
+<StructureSection load='2fwl' size='340' side='right'caption='[[2fwl]]' 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'>[[2fwl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FWL 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">Solution NMR, 3 models</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CUA:DINUCLEAR+COPPER+ION'>CUA</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
-{{STRUCTURE_2fwl|  PDB=2fwl  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fwl OCA], [https://pdbe.org/2fwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fwl RCSB], [https://www.ebi.ac.uk/pdbsum/2fwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fwl ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/COX2_THETH COX2_THETH] Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
+== 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/fw/2fwl_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=2fwl ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The structural analysis of the redox complex between the soluble cytochrome c552 and the membrane-integral cytochrome ba3 oxidase of Thermus thermophilus is complicated by the transient nature of this protein-protein interaction. Using NMR-based chemical shift perturbation mapping, however, we identified the contact regions between cytochrome c552 and the CuA domain, the fully functional water-soluble fragment of subunit II of the ba3 oxidase. First we determined the complete backbone resonance assignments of both proteins for each redox state. Subsequently, two-dimensional [15N,1H]TROSY spectra recorded for each redox partner both in free and complexed state indicated those surface residues affected by complex formation between the two proteins. This chemical shift analysis performed for both redox states provided a topological description of the contact surface on each partner molecule. Remarkably, very pronounced indirect effects, which were observed on the back side of the heme cleft only in the reduced state, suggested that alterations of the electron distribution in the porphyrin ring due to formation of the protein-protein complex are apparently sensed even beyond the heme propionate groups. The contact residues of each redox partner, as derived from the chemical shift perturbation mapping, were employed for a protein-protein docking calculation that provided a structure ensemble of 10 closely related conformers representing the complex between cytochrome c552 and the CuA domain. Based on these structures, the electron transfer pathway from the heme of cytochrome c552 to the CuA center of the ba3 oxidase has been predicted.
-===The cytochrome c552/CuA complex from Thermus thermophilus===
+The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase. A combined NMR and computational approach.,Muresanu L, Pristovsek P, Lohr F, Maneg O, Mukrasch MD, Ruterjans H, Ludwig B, Lucke C J Biol Chem. 2006 May 19;281(20):14503-13. Epub 2006 Mar 22. PMID:16554303<ref>PMID:16554303</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2fwl" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16554303}}, adds the Publication Abstract to the page
+*[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16554303 is the PubMed ID number.
+*[[Cytochrome c oxidase 3D structures|Cytochrome c oxidase 3D structures]]
--->
+== References ==
-{{ABSTRACT_PUBMED_16554303}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-FWL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FWL OCA].
+[[Category: Large Structures]]
+[[Category: Thermus thermophilus HB8]]
-==Reference==
+[[Category: Loehr F]]
-The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase. A combined NMR and computational approach., Muresanu L, Pristovsek P, Lohr F, Maneg O, Mukrasch MD, Ruterjans H, Ludwig B, Lucke C, J Biol Chem. 2006 May 19;281(20):14503-13. Epub 2006 Mar 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16554303 16554303]
+[[Category: Ludwig B]]
-[[Category: Cytochrome-c oxidase]]
+[[Category: Luecke C]]
-[[Category: Protein complex]]
+[[Category: Maneg O]]
-[[Category: Thermus thermophilus]]
+[[Category: Mukrasch MD]]
-[[Category: Loehr, F.]]
+[[Category: Muresanu L]]
-[[Category: Ludwig, B.]]
+[[Category: Pristovsek P]]
-[[Category: Luecke, C.]]
+[[Category: Rueterjans H]]
-[[Category: Maneg, O.]]
-[[Category: Mukrasch, M D.]]
-[[Category: Muresanu, L.]]
-[[Category: Pristovsek, P.]]
-[[Category: Rueterjans, H.]]
-[[Category: Docking calculation]]
-[[Category: Electron transfer pathway]]
-[[Category: Redox protein complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:25:06 2008''