1xmd

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[[Image:1xmd.gif|left|200px]]
 
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{{Structure
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==M335V mutant structure of mouse carnitine octanoyltransferase==
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|PDB= 1xmd |SIZE=350|CAPTION= <scene name='initialview01'>1xmd</scene>, resolution 2.10&Aring;
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<StructureSection load='1xmd' size='340' side='right'caption='[[1xmd]], [[Resolution|resolution]] 2.10&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'>[[1xmd]] 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=1XMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XMD 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]] 2.1&#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=1xmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmd OCA], [https://pdbe.org/1xmd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xmd RCSB], [https://www.ebi.ac.uk/pdbsum/1xmd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xmd ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1xl7|1XL7]], [[1xl8|1XL8]], [[1xmc|1XMC]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmd OCA], [http://www.ebi.ac.uk/pdbsum/1xmd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xmd 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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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xm/1xmd_consurf.spt"</scriptWhenChecked>
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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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</jmolCheckbox>
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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=1xmd ConSurf].
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<div style="clear:both"></div>
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'''M335V mutant structure of mouse carnitine octanoyltransferase'''
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==See Also==
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*[[Butyrylcholinesterase 3D structures|Butyrylcholinesterase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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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[[Category: Large Structures]]
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==About this Structure==
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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].
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==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://www.ncbi.nlm.nih.gov/pubmed/15492013 15492013]
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[[Category: Carnitine O-octanoyltransferase]]
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[[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

M335V mutant structure of mouse carnitine octanoyltransferase

PDB ID 1xmd

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