2h3p: Difference between revisions

Revision as of 11:28, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2h3p.png

Template:STRUCTURE 2h3p

Crystal structure of murine carnitine acetyltransferase in complex with carnitine and acetyl-CoACrystal structure of murine carnitine acetyltransferase in complex with carnitine and acetyl-CoA

Template:ABSTRACT PUBMED 16870616

About this StructureAbout this Structure

2H3P is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of murine carnitine acetyltransferase in ternary complexes with its substrates., Hsiao YS, Jogl G, Tong L, J Biol Chem. 2006 Sep 22;281(38):28480-7. Epub 2006 Jul 26. PMID:16870616

Page seeded by OCA on Tue Jul 29 11:28:45 2008

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OCA

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-'''Crystal structure of murine carnitine acetyltransferase in complex with carnitine and acetyl-CoA'''
+===Crystal structure of murine carnitine acetyltransferase in complex with carnitine and acetyl-CoA===
-==Overview==
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-Carnitine acyltransferases catalyze the reversible exchange of acyl groups between coenzyme A (CoA) and carnitine. They have important roles in many cellular processes, especially the oxidation of long-chain fatty acids in the mitochondria for energy production, and are attractive targets for drug discovery against diabetes and obesity. To help define in molecular detail the catalytic mechanism of these enzymes, we report here the high resolution crystal structure of wild-type murine carnitine acetyltransferase (CrAT) in a ternary complex with its substrates acetyl-CoA and carnitine, and the structure of the S554A/M564G double mutant in a ternary complex with the substrates CoA and hexanoylcarnitine. Detailed analyses suggest that these structures may be good mimics for the Michaelis complexes for the forward and reverse reactions of the enzyme, representing the first time that such complexes of CrAT have been studied in molecular detail. The structural information provides significant new insights into the catalytic mechanism of CrAT and possibly carnitine acyltransferases in general.
+The line below this paragraph, {{ABSTRACT_PUBMED_16870616}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16870616 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16870616}}
 ==About this Structure==
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 [[Category: Tong, L.]]
 [[Category: Carnitine acyltransferase]]
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