2H3U

Crystal structure of murine carnitine acetyltransferase in complex with carnitine and CoA

Summary for 2H3U

• Entry DOI: 10.2210/pdb2h3u/pdb
• Related: 1NDB 1NDF 1NDI 1T7N 1T7O 1T7Q 2H3P 2H3W
• Descriptor: carnitine acetyltransferase, COENZYME A, CARNITINE, ... (4 entities in total)
• Functional Keywords: carnitine acyltransferase, transferase
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 2
• Total formula weight: 137935.25

Authors

Hsiao, Y.S.,Jogl, G.,Tong, L. (deposition date: 2006-05-23, release date: 2006-08-01, Last modification date: 2024-02-14)

Primary citation

Hsiao, Y.-S.,Jogl, G.,Tong, L.
Crystal structures of murine carnitine acetyltransferase in ternary complexes with its substrates
J.Biol.Chem., 281:28480-28487, 2006

PubMed Abstract: 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.

PubMed: 16870616
DOI: 10.1074/jbc.M602622200

Experimental method

X-RAY DIFFRACTION (1.9 Å)