4cts

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[[Image:4cts.gif|left|200px]]
 
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==CRYSTAL STRUCTURE ANALYSIS AND MOLECULAR MODEL OF A COMPLEX OF CITRATE SYNTHASE WITH OXALOACETATE AND S-ACETONYL-COENZYME A==
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The line below this paragraph, containing "STRUCTURE_4cts", creates the "Structure Box" on the page.
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<StructureSection load='4cts' size='340' side='right'caption='[[4cts]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[4cts]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CTS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene></td></tr>
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{{STRUCTURE_4cts| PDB=4cts | SCENE= }}
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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=4cts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cts OCA], [https://pdbe.org/4cts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cts RCSB], [https://www.ebi.ac.uk/pdbsum/4cts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cts ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CISY_PIG CISY_PIG]
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== Evolutionary Conservation ==
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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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ct/4cts_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=4cts ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE ANALYSIS AND MOLECULAR MODEL OF A COMPLEX OF CITRATE SYNTHASE WITH OXALOACETATE AND S-ACETONYL-COENZYME A'''
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==See Also==
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*[[Citrate Synthase 3D structures|Citrate Synthase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The crystal structure of the complex of pig heart citrate synthase and oxaloacetate in the presence of the potent inhibitor S-acetonyl coenzyme A has been determined at a nominal resolution of 2.9 A by Patterson search techniques and refined by restrained crystallographic refinement. The complex crystallizes in the presence of polyvinylpyrrolidone in space group P4(3)2(1)2 with a = 101.5 A and c = 224.6 A, with one dimeric molecule of molecular weight 100,000 in the asymmetric unit. The crystallographic R factor is 0.194 for the 14,332 unique reflections between 6.0 and 2.9 A resolution. The structures of two forms of citrate synthase in the presence and absence of product molecules have been determined recently and shown to differ in the relative arrangement of the large and small domains ("closed" and "open" forms). The third crystal form described here is also closed, but there is substantial rearrangement within the small domain relative to either of the other crystal forms. We conclude that this is a third structural state of the enzyme, and catalytic activity of the enzyme depends on structural changes during the course of the reaction affecting domain conformation also. The three structures are compared, and it is shown that the large domain is considerably more rigid than the small domain. The conformation of the small domain adapts to the ligand. The inhibitor, and the "coenzyme-A-binding segment" of the enzyme are disordered. No electron density is observed for the inhibitor, and only weak density for the coenzyme-A-binding segment. Electron density for oxaloacetate is well defined. It binds in a very similar manner to citrate.
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[[Category: Large Structures]]
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==About this Structure==
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4CTS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CTS OCA].
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==Reference==
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Crystal structure analysis and molecular model of a complex of citrate synthase with oxaloacetate and S-acetonyl-coenzyme A., Wiegand G, Remington S, Deisenhofer J, Huber R, J Mol Biol. 1984 Mar 25;174(1):205-19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/6716477 6716477]
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[[Category: Single protein]]
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Huber, R.]]
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[[Category: Huber R]]
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[[Category: Remington, S.]]
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[[Category: Remington S]]
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[[Category: Wiegand, G.]]
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[[Category: Wiegand G]]
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[[Category: Oxo-acid-lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:22:49 2008''
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Current revision

CRYSTAL STRUCTURE ANALYSIS AND MOLECULAR MODEL OF A COMPLEX OF CITRATE SYNTHASE WITH OXALOACETATE AND S-ACETONYL-COENZYME A

PDB ID 4cts

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