1ndf
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(New page: 200px<br /><applet load="1ndf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ndf, resolution 1.90Å" /> '''Carnitine Acetyltran...)
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Revision as of 20:02, 20 November 2007
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Carnitine Acetyltransferase in Complex with Carnitine
Overview
Carnitine acyltransferases have crucial roles in the transport of fatty, acids for beta-oxidation. Dysregulation of these enzymes can lead to, serious diseases in humans, and they are targets for therapeutic, development against diabetes. We report the crystal structures of murine, carnitine acetyltransferase (CRAT), alone and in complex with its, substrate carnitine or CoA. The structure contains two domains., Surprisingly, these two domains share the same backbone fold, which is, also similar to that of chloramphenicol acetyltransferase and, dihydrolipoyl transacetylase. The active site is located at the interface, between the two domains. Carnitine and CoA are bound in deep channels in, the enzyme, on opposite sides of the catalytic His343 residue. The, structural information provides a molecular basis for understanding the, catalysis by carnitine acyltransferases and for designing their, inhibitors. Specifically, our structural information suggests that the, substrate carnitine may assist the catalysis by stabilizing the oxyanion, in the reaction intermediate.
About this Structure
1NDF is a Single protein structure of sequence from Mus musculus with 152 as ligand. Active as Carnitine O-acetyltransferase, with EC number 2.3.1.7 Full crystallographic information is available from OCA.
Reference
Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport., Jogl G, Tong L, Cell. 2003 Jan 10;112(1):113-22. PMID:12526798
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