1xmc

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[[Image:1xmc.gif|left|200px]]
 
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{{Structure
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==C323M mutant structure of mouse carnitine octanoyltransferase==
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|PDB= 1xmc |SIZE=350|CAPTION= <scene name='initialview01'>1xmc</scene>, resolution 2.00&Aring;
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<StructureSection load='1xmc' size='340' side='right'caption='[[1xmc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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<table><tr><td colspan='2'>[[1xmc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XMC FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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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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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmc OCA], [https://pdbe.org/1xmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xmc RCSB], [https://www.ebi.ac.uk/pdbsum/1xmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xmc ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1xl7|1XL7]], [[1xl8|1XL8]], [[1xmd|1XMD]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmc OCA], [http://www.ebi.ac.uk/pdbsum/1xmc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xmc RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/OCTC_MOUSE OCTC_MOUSE] Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate (By similarity).
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== Evolutionary Conservation ==
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'''C323M mutant structure of mouse carnitine octanoyltransferase'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xm/1xmc_consurf.spt"</scriptWhenChecked>
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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.
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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1XMC 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=1XMC OCA].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xmc ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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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]
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</StructureSection>
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[[Category: Carnitine O-octanoyltransferase]]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Hsiao YS]]
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[[Category: Hsiao, Y S.]]
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[[Category: Jogl G]]
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[[Category: Jogl, G.]]
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[[Category: Tong L]]
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[[Category: Tong, L.]]
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[[Category: carnitine]]
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[[Category: hepe]]
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[[Category: mpd]]
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[[Category: mutant]]
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[[Category: octanoyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:51:39 2008''
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Current revision

C323M mutant structure of mouse carnitine octanoyltransferase

PDB ID 1xmc

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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