1xmd

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[[Image:1xmd.gif|left|200px]]<br /><applet load="1xmd" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1xmd.gif|left|200px]]
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caption="1xmd, resolution 2.10&Aring;" />
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'''M335V mutant structure of mouse carnitine octanoyltransferase'''<br />
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{{Structure
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|PDB= 1xmd |SIZE=350|CAPTION= <scene name='initialview01'>1xmd</scene>, resolution 2.10&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Carnitine_O-octanoyltransferase Carnitine O-octanoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.137 2.3.1.137]
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|GENE= Crot, Cot ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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}}
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'''M335V mutant structure of mouse carnitine octanoyltransferase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1XMD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=EPE:'>EPE</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carnitine_O-octanoyltransferase Carnitine O-octanoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.137 2.3.1.137] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMD OCA].
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1XMD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMD OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15492013 15492013]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15492013 15492013]
[[Category: Carnitine O-octanoyltransferase]]
[[Category: Carnitine O-octanoyltransferase]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: MPD]]
[[Category: MPD]]
[[Category: carnitine]]
[[Category: carnitine]]
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[[Category: hepes]]
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[[Category: hepe]]
[[Category: mpd]]
[[Category: mpd]]
[[Category: mutant]]
[[Category: mutant]]
[[Category: octanoyltransferase]]
[[Category: octanoyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:56:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:11:45 2008''

Revision as of 13:11, 20 March 2008

Image:1xmd.gif


PDB ID 1xmd

Drag the structure with the mouse to rotate
, resolution 2.10Å
Ligands: and
Gene: Crot, Cot (Mus musculus)
Activity: Carnitine O-octanoyltransferase, with EC number 2.3.1.137
Coordinates: save as pdb, mmCIF, xml



M335V 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.

About this Structure

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

Reference

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

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