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1ndb

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[[Image:1ndb.gif|left|200px]]
 
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{{Structure
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==Crystal structure of Carnitine Acetyltransferase==
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|PDB= 1ndb |SIZE=350|CAPTION= <scene name='initialview01'>1ndb</scene>, resolution 1.80&Aring;
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<StructureSection load='1ndb' size='340' side='right'caption='[[1ndb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1ndb]] 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=1NDB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NDB FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Carnitine_O-acetyltransferase Carnitine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.7 2.3.1.7]
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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]] 1.8&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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}}
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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=1ndb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ndb OCA], [https://pdbe.org/1ndb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ndb RCSB], [https://www.ebi.ac.uk/pdbsum/1ndb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ndb 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/nd/1ndb_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=1ndb ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of Carnitine Acetyltransferase'''
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==See Also==
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*[[Carnitine acetyltransferase|Carnitine acetyltransferase]]
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__TOC__
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==Overview==
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</StructureSection>
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Carnitine acyltransferases have crucial roles in the transport of fatty acids for beta-oxidation. Dysregulation of these enzymes can lead to serious diseases in humans, and they are targets for therapeutic development against diabetes. We report the crystal structures of murine carnitine acetyltransferase (CRAT), alone and in complex with its substrate carnitine or CoA. The structure contains two domains. Surprisingly, these two domains share the same backbone fold, which is also similar to that of chloramphenicol acetyltransferase and dihydrolipoyl transacetylase. The active site is located at the interface between the two domains. Carnitine and CoA are bound in deep channels in the enzyme, on opposite sides of the catalytic His343 residue. The structural information provides a molecular basis for understanding the catalysis by carnitine acyltransferases and for designing their inhibitors. Specifically, our structural information suggests that the substrate carnitine may assist the catalysis by stabilizing the oxyanion in the reaction intermediate.
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[[Category: Large Structures]]
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==About this Structure==
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1NDB 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=1NDB OCA].
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==Reference==
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Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport., Jogl G, Tong L, Cell. 2003 Jan 10;112(1):113-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12526798 12526798]
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[[Category: Carnitine O-acetyltransferase]]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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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: acetyl transfer]]
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[[Category: coa]]
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[[Category: coenzyme some]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:55:23 2008''
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Current revision

Crystal structure of Carnitine Acetyltransferase

PDB ID 1ndb

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