1ndf

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{{Seed}}
 
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[[Image:1ndf.png|left|200px]]
 
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==Carnitine Acetyltransferase in Complex with Carnitine==
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The line below this paragraph, containing "STRUCTURE_1ndf", creates the "Structure Box" on the page.
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<StructureSection load='1ndf' size='340' side='right'caption='[[1ndf]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ndf]] 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=1NDF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NDF FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.9&#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></td></tr>
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{{STRUCTURE_1ndf| PDB=1ndf | SCENE= }}
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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=1ndf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ndf OCA], [https://pdbe.org/1ndf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ndf RCSB], [https://www.ebi.ac.uk/pdbsum/1ndf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ndf 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/1ndf_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=1ndf 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 Carnitine===
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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 1ndf" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12526798}}, adds the Publication Abstract to the page
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*[[Carnitine acetyltransferase|Carnitine acetyltransferase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12526798 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12526798}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1NDF is a 2 chains structure of sequences 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=1NDF OCA].
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==Reference==
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<ref group="xtra">PMID:12526798</ref><references group="xtra"/>
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[[Category: Carnitine O-acetyltransferase]]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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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 Tue Feb 17 19:11:17 2009''
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Current revision

Carnitine Acetyltransferase in Complex with Carnitine

PDB ID 1ndf

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