1xmc: Difference between revisions

Revision as of 12:03, 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:1xmc.png

Template:STRUCTURE 1xmc

C323M mutant structure of mouse carnitine octanoyltransferaseC323M mutant structure of mouse carnitine octanoyltransferase

Template:ABSTRACT PUBMED 15492013

About this StructureAbout this Structure

1XMC is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of mouse carnitine octanoyltransferase and molecular determinants of substrate selectivity., Jogl G, Hsiao YS, Tong L, J Biol Chem. 2005 Jan 7;280(1):738-44. Epub 2004 Oct 17. PMID:15492013

Page seeded by OCA on Tue Jul 29 12:02:59 2008

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OCA

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-'''C323M mutant structure of mouse carnitine octanoyltransferase'''
+===C323M mutant structure of mouse carnitine octanoyltransferase===
-==Overview==
+<!--
-Carnitine acyltransferases have crucial functions in fatty acid metabolism. Members of this enzyme family show distinctive substrate preferences for short-, medium- or long-chain fatty acids. The molecular mechanism for this substrate selectivity is not clear as so far only the structure of carnitine acetyltransferase has been determined. To further our understanding of these important enzymes, we report here the crystal structures at up to 2.0-A resolution of mouse carnitine octanoyltransferase alone and in complex with the substrate octanoylcarnitine. The structures reveal significant differences in the acyl group binding pocket between carnitine octanoyltransferase and carnitine acetyltransferase. Amino acid substitutions and structural changes produce a larger hydrophobic pocket that binds the octanoyl group in an extended conformation. Mutation of a single residue (Gly-553) in this pocket can change the substrate preference between short- and medium-chain acyl groups. The side chains of Cys-323 and Met-335 at the bottom of this pocket assume dual conformations in the substrate complex, and mutagenesis studies suggest that the Met-335 residue is important for catalysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_15492013}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15492013}}
 ==About this Structure==
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 [[Category: Mutant]]
 [[Category: Octanoyltransferase]]
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