5cts: Difference between revisions

Revision as of 13:59, 3 July 2008

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File:5cts.png

Template:STRUCTURE 5cts

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

Template:ABSTRACT PUBMED 2337600

About this StructureAbout this Structure

5CTS is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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-[[Image:5cts.gif|left|200px]]
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 {{STRUCTURE_5cts|  PDB=5cts  |  SCENE=  }}
-'''PROPOSED MECHANISM FOR THE CONDENSATION REACTION OF CITRATE SYNTHASE. 1.9-ANGSTROMS STRUCTURE OF THE TERNARY COMPLEX WITH OXALOACETATE AND CARBOXYMETHYL COENZYME A'''
+===PROPOSED MECHANISM FOR THE CONDENSATION REACTION OF CITRATE SYNTHASE. 1.9-ANGSTROMS STRUCTURE OF THE TERNARY COMPLEX WITH OXALOACETATE AND CARBOXYMETHYL COENZYME A===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_2337600}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 2337600 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_2337600}}
 ==About this Structure==
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 [[Category: Remington, S J.]]
 [[Category: Oxo-acid-lyase]]
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