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5cts

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[[Image:5cts.gif|left|200px]]
 
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{{Structure
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==PROPOSED MECHANISM FOR THE CONDENSATION REACTION OF CITRATE SYNTHASE. 1.9-ANGSTROMS STRUCTURE OF THE TERNARY COMPLEX WITH OXALOACETATE AND CARBOXYMETHYL COENZYME A==
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|PDB= 5cts |SIZE=350|CAPTION= <scene name='initialview01'>5cts</scene>, resolution 1.9&Aring;
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<StructureSection load='5cts' size='340' side='right'caption='[[5cts]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene> and <scene name='pdbligand=CMC:CARBOXYMETHYL COENZYME *A'>CMC</scene>
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<table><tr><td colspan='2'>[[5cts]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CTS FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Citrate_(Si)-synthase Citrate (Si)-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.1 2.3.3.1]
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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]] 1.9&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMC:CARBOXYMETHYL+COENZYME+*A'>CMC</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene></td></tr>
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}}
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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=5cts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cts OCA], [https://pdbe.org/5cts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cts RCSB], [https://www.ebi.ac.uk/pdbsum/5cts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cts ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CISY_CHICK CISY_CHICK]
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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/5cts_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=5cts ConSurf].
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<div style="clear:both"></div>
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'''PROPOSED MECHANISM FOR THE CONDENSATION REACTION OF CITRATE SYNTHASE. 1.9-ANGSTROMS STRUCTURE OF THE TERNARY COMPLEX WITH OXALOACETATE AND CARBOXYMETHYL COENZYME A'''
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==See Also==
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*[[Citrate Synthase|Citrate Synthase]]
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*[[Citrate Synthase 3D structures|Citrate Synthase 3D structures]]
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==Overview==
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__TOC__
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The crystal structure of the ternary complex citrate synthase-oxaloacetate-carboxymethyl coenzyme A has been solved to a resolution of 1.9 A and refined to a conventional crystallographic R factor of 0.185. The structure resembles a proposed transition state of the condensation reaction and suggests that the condensation reaction proceeds through a neutral enol rather than an enolate intermediate. A mechanism for the condensation reaction is proposed which involves the participation of three key catalytic groups (Asp 375, His 274, and His 320) in two distinct steps. The proposed mechanism invokes concerted general acid-base catalysis twice to explain both the energetics of the reaction and the experimentally observed inversion of stereochemistry at the attacking carbon atom.
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</StructureSection>
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==About this Structure==
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5CTS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CTS OCA].
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==Reference==
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Proposed mechanism for the condensation reaction of citrate synthase: 1.9-A structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A., Karpusas M, Branchaud B, Remington SJ, Biochemistry. 1990 Mar 6;29(9):2213-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2337600 2337600]
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[[Category: Citrate (Si)-synthase]]
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Branchaud, B.]]
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[[Category: Branchaud B]]
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[[Category: Karpusas, M.]]
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[[Category: Karpusas M]]
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[[Category: Remington, S J.]]
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[[Category: Remington SJ]]
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[[Category: CMC]]
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[[Category: OAA]]
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[[Category: oxo-acid-lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:11:50 2008''
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Current revision

PROPOSED MECHANISM FOR THE CONDENSATION REACTION OF CITRATE SYNTHASE. 1.9-ANGSTROMS STRUCTURE OF THE TERNARY COMPLEX WITH OXALOACETATE AND CARBOXYMETHYL COENZYME A

PDB ID 5cts

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