2jqr: Difference between revisions

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-[[Image:2jqr.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2jqr", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
--->
-{{STRUCTURE_2jqr|  PDB=2jqr  |  SCENE=  }}
-'''Solution model of crosslinked complex of cytochrome c and adrenodoxin'''
+==Solution model of crosslinked complex of cytochrome c and adrenodoxin==
+<StructureSection load='2jqr' size='340' side='right'caption='[[2jqr]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2jqr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JQR FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jqr OCA], [https://pdbe.org/2jqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jqr RCSB], [https://www.ebi.ac.uk/pdbsum/2jqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jqr ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CYC1_YEAST CYC1_YEAST] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
+== 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/jq/2jqr_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=2jqr ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+In the general view of protein-complex formation, a transient and dynamic encounter complex proceeds to form a more stable, well-defined, and active form. In weak protein complexes, however, the encounter state can represent a significant population of the complex. The redox proteins adrenodoxin (Adx) and cytochrome c (C c) associate to form such a weak and short-lived complex, which is nevertheless active in electron transfer. To study the conformational freedom within the protein complex, the native complex has been compared to a cross-linked counterpart by using solution scattering and NMR spectroscopy. Oligomerization behavior of the native complex in solution revealed by small-angle X-ray scattering indicates a stochastic nature of complex formation. For the cross-linked complex, interprotein paramagnetic effects are observed, whereas for the native complex, extensive averaging occurs, consistent with multiple orientations of the proteins within the complex. Simulations show that C c samples about half of the surface area of adrenodoxin. It is concluded that the complex of Adx/C c is entirely dynamic and can be considered as a pure encounter complex.
-==Overview==
+Dynamics in a pure encounter complex of two proteins studied by solution scattering and paramagnetic NMR spectroscopy.,Xu X, Reinle W, Hannemann F, Konarev PV, Svergun DI, Bernhardt R, Ubbink M J Am Chem Soc. 2008 May 21;130(20):6395-403. Epub 2008 Apr 26. PMID:18439013<ref>PMID:18439013</ref>
-In the general view of protein-complex formation, a transient and dynamic encounter complex proceeds to form a more stable, well-defined, and active form. In weak protein complexes, however, the encounter state can represent a significant population of the complex. The redox proteins adrenodoxin (Adx) and cytochrome c (C c) associate to form such a weak and short-lived complex, which is nevertheless active in electron transfer. To study the conformational freedom within the protein complex, the native complex has been compared to a cross-linked counterpart by using solution scattering and NMR spectroscopy. Oligomerization behavior of the native complex in solution revealed by small-angle X-ray scattering indicates a stochastic nature of complex formation. For the cross-linked complex, interprotein paramagnetic effects are observed, whereas for the native complex, extensive averaging occurs, consistent with multiple orientations of the proteins within the complex. Simulations show that C c samples about half of the surface area of adrenodoxin. It is concluded that the complex of Adx/C c is entirely dynamic and can be considered as a pure encounter complex.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-JQR is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JQR OCA].
+</div>
+<div class="pdbe-citations 2jqr" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Dynamics in a pure encounter complex of two proteins studied by solution scattering and paramagnetic NMR spectroscopy., Xu X, Reinle W, Hannemann F, Konarev PV, Svergun DI, Bernhardt R, Ubbink M, J Am Chem Soc. 2008 May 21;130(20):6395-403. Epub 2008 Apr 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18439013 18439013]
+*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
+*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Bos taurus]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Bernhardt, R.]]
+[[Category: Bernhardt R]]
-[[Category: Hannemann, F.]]
+[[Category: Hannemann F]]
-[[Category: Konarev, P V.]]
+[[Category: Konarev PV]]
-[[Category: Reinle, W.]]
+[[Category: Reinle W]]
-[[Category: Svergun, D I.]]
+[[Category: Svergun DI]]
-[[Category: Ubbink, M.]]
+[[Category: Ubbink M]]
-[[Category: Xu, X.]]
+[[Category: Xu X]]
-[[Category: 2fe2s ferredoxin]]
-[[Category: Adrenodoxin]]
-[[Category: Crosslinked complex]]
-[[Category: Cytochrome c]]
-[[Category: Electron transport]]
-[[Category: Encounter complex]]
-[[Category: Paramagnetic relaxation enhancement]]
-[[Category: Pseudocontact shift]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 10:54:17 2008''