6cts: Difference between revisions

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[[Image:6cts.~~gif~~|left|200px]]

[[Image:6cts.png|left|200px]]

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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~~'''~~

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

~~==Overview==~~

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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.~~

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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==About this Structure==

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[[Category: Remington, S J.]]

[[Category: Oxo-acid-lyase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May~~ ~~4 22~~:40:01 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 14:17:13 2008''

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-[[Image:6cts.gif|left|200px]]
+{{Seed}}
+[[Image:6cts.png|left|200px]]
 <!--
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 {{STRUCTURE_6cts|  PDB=6cts  |  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.
+-->
+{{ABSTRACT_PUBMED_2337600}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Remington, S J.]]
 [[Category: Oxo-acid-lyase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:40:01 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 14:17:13 2008''