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[[Image: | ==PROPOSED MECHANISM FOR THE CONDENSATION REACTION OF CITRATE SYNTHASE. 1.9-ANGSTROMS STRUCTURE OF THE TERNARY COMPLEX WITH OXALOACETATE AND CARBOXYMETHYL COENZYME A== | ||
<StructureSection load='6cts' size='340' side='right' caption='[[6cts]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6cts]] is a 1 chain structure with 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=6CTS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CTS FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIC:CITRYL-THIOETHER-COENZYME+*A'>CIC</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6cts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cts OCA], [http://www.rcsb.org/pdb/explore.do?structureId=6cts RCSB], [http://www.ebi.ac.uk/pdbsum/6cts PDBsum]</span></td></tr> | |||
</table> | |||
== 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/ct/6cts_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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:2337600<ref>PMID:2337600</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Citrate Synthase|Citrate Synthase]] | *[[Citrate Synthase|Citrate Synthase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Branchaud, B | [[Category: Branchaud, B]] | ||
[[Category: Karpusas, M | [[Category: Karpusas, M]] | ||
[[Category: Remington, S J | [[Category: Remington, S J]] | ||
[[Category: Oxo-acid-lyase]] | [[Category: Oxo-acid-lyase]] | ||
Revision as of 13:41, 20 November 2014
PROPOSED MECHANISM FOR THE CONDENSATION REACTION OF CITRATE SYNTHASE. 1.9-ANGSTROMS STRUCTURE OF THE TERNARY COMPLEX WITH OXALOACETATE AND CARBOXYMETHYL COENZYME APROPOSED MECHANISM FOR THE CONDENSATION REACTION OF CITRATE SYNTHASE. 1.9-ANGSTROMS STRUCTURE OF THE TERNARY COMPLEX WITH OXALOACETATE AND CARBOXYMETHYL COENZYME A
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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:2337600[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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