1ndi

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[[Image:1ndi.gif|left|200px]]
 
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{{Structure
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==Carnitine Acetyltransferase in complex with CoA==
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|PDB= 1ndi |SIZE=350|CAPTION= <scene name='initialview01'>1ndi</scene>, resolution 2.30&Aring;
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<StructureSection load='1ndi' size='340' side='right'caption='[[1ndi]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene>
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<table><tr><td colspan='2'>[[1ndi]] 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=1NDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NDI FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </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]] 2.3&#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=COA:COENZYME+A'>COA</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=1ndi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ndi OCA], [https://pdbe.org/1ndi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ndi RCSB], [https://www.ebi.ac.uk/pdbsum/1ndi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ndi ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1ndb|1NDB]], [[1ndf|1NDF]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ndi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ndi OCA], [http://www.ebi.ac.uk/pdbsum/1ndi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ndi RCSB]</span>
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== Function ==
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}}
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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/1ndi_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=1ndi ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''Carnitine Acetyltransferase in complex with CoA'''
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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:12526798<ref>PMID:12526798</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ndi" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Carnitine acetyltransferase|Carnitine acetyltransferase]]
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== References ==
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==About this Structure==
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<references/>
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1NDI 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=1NDI OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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 Sun Mar 30 22:28:51 2008''
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Current revision

Carnitine Acetyltransferase in complex with CoA

PDB ID 1ndi

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