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2h3p

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(New page: 200px<br /><applet load="2h3p" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h3p, resolution 2.20&Aring;" /> '''Crystal structure of...)
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[[Image:2h3p.gif|left|200px]]<br /><applet load="2h3p" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2h3p, resolution 2.20&Aring;" />
 
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'''Crystal structure of murine carnitine acetyltransferase in complex with carnitine and acetyl-CoA'''<br />
 
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==Overview==
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==Crystal structure of murine carnitine acetyltransferase in complex with carnitine and acetyl-CoA==
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Carnitine acyltransferases catalyze the reversible exchange of acyl groups, between coenzyme A (CoA) and carnitine. They have important roles in many, cellular processes, especially the oxidation of long-chain fatty acids in, the mitochondria for energy production, and are attractive targets for, drug discovery against diabetes and obesity. To help define in molecular, detail the catalytic mechanism of these enzymes, we report here the high, resolution crystal structure of wild-type murine carnitine, acetyltransferase (CrAT) in a ternary complex with its substrates, acetyl-CoA and carnitine, and the structure of the S554A/M564G double, mutant in a ternary complex with the substrates CoA and hexanoylcarnitine., Detailed analyses suggest that these structures may be good mimics for the, Michaelis complexes for the forward and reverse reactions of the enzyme, representing the first time that such complexes of CrAT have been studied, in molecular detail. The structural information provides significant new, insights into the catalytic mechanism of CrAT and possibly carnitine, acyltransferases in general.
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<StructureSection load='2h3p' size='340' side='right'caption='[[2h3p]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2h3p]] 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=2H3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H3P FirstGlance]. <br>
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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]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=152:CARNITINE'>152</scene>, <scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
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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=2h3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h3p OCA], [https://pdbe.org/2h3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h3p RCSB], [https://www.ebi.ac.uk/pdbsum/2h3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h3p ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CACP_MOUSE CACP_MOUSE] Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria.
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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/h3/2h3p_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=2h3p ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2H3P 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 COA, ACO and 152 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2H3P OCA].
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*[[Carnitine acetyltransferase|Carnitine acetyltransferase]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structures of murine carnitine acetyltransferase in ternary complexes with its substrates., Hsiao YS, Jogl G, Tong L, J Biol Chem. 2006 Sep 22;281(38):28480-7. Epub 2006 Jul 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16870616 16870616]
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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: 152]]
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[[Category: ACO]]
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[[Category: COA]]
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[[Category: carnitine acyltransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:31:57 2007''
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Current revision

Crystal structure of murine carnitine acetyltransferase in complex with carnitine and acetyl-CoA

PDB ID 2h3p

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