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1nm8

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(New page: 200px<br /> <applet load="1nm8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nm8, resolution 1.6&Aring;" /> '''Structure of Human C...)
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[[Image:1nm8.gif|left|200px]]<br />
 
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<applet load="1nm8" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1nm8, resolution 1.6&Aring;" />
 
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'''Structure of Human Carnitine Acetyltransferase: Molecular Basis for Fatty Acyl Transfer'''<br />
 
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==Overview==
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==Structure of Human Carnitine Acetyltransferase: Molecular Basis for Fatty Acyl Transfer==
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Carnitine acyltransferases are a family of ubiquitous enzymes that play a, pivotal role in cellular energy metabolism. We report here the x-ray, structure of human carnitine acetyltransferase to a 1.6-A resolution. This, structure reveals a monomeric protein of two equally sized alpha/beta, domains. Each domain is shown to have a partially similar fold to other, known but oligomeric enzymes that are also involved in group-transfer, reactions. The unique monomeric arrangement of the two domains constitutes, a central narrow active site tunnel, indicating a likely universal feature, for all members of the carnitine acyltransferase family. Superimposition, of the substrate complex of a related protein, dihydrolipoyl, trans-acetylase, reveals that both substrates localize to the active site, tunnel of human carnitine acetyltransferase, suggesting the location of, the ligand binding sites for carnitine and coenzyme A. Most significantly, this structure provides critical insights into the molecular basis for, fatty acyl chain transfer and a possible common mechanism among a wide, range of acyltransferases utilizing a catalytic dyad.
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<StructureSection load='1nm8' size='340' side='right'caption='[[1nm8]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1nm8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NM8 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]] 1.6&#8491;</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=1nm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nm8 OCA], [https://pdbe.org/1nm8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nm8 RCSB], [https://www.ebi.ac.uk/pdbsum/1nm8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nm8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CACP_HUMAN CACP_HUMAN] 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/nm/1nm8_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=1nm8 ConSurf].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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Known disease associated with this structure: Carnitine acetyltransferase deficiency (1) OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600184 600184]]
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*[[Carnitine acetyltransferase|Carnitine acetyltransferase]]
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__TOC__
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==About this Structure==
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</StructureSection>
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1NM8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NM8 OCA].
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==Reference==
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Structure of human carnitine acetyltransferase. Molecular basis for fatty acyl transfer., Wu D, Govindasamy L, Lian W, Gu Y, Kukar T, Agbandje-McKenna M, McKenna R, J Biol Chem. 2003 Apr 11;278(15):13159-65. Epub 2003 Jan 31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12562770 12562770]
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[[Category: Carnitine O-acetyltransferase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Agbandje-McKenna, M.]]
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[[Category: Agbandje-McKenna M]]
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[[Category: Govindasamy, L.]]
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[[Category: Govindasamy L]]
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[[Category: Gu, Y.]]
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[[Category: Gu Y]]
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[[Category: Kukar, T.]]
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[[Category: Kukar T]]
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[[Category: Lian, W.]]
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[[Category: Lian W]]
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[[Category: McKenna, R.]]
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[[Category: McKenna R]]
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[[Category: Wu, D.]]
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[[Category: Wu D]]
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[[Category: anti-parallel beta-strand]]
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[[Category: two equally sized domains]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:22:37 2007''
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Current revision

Structure of Human Carnitine Acetyltransferase: Molecular Basis for Fatty Acyl Transfer

PDB ID 1nm8

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