2h3p: Difference between revisions

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<StructureSection load='2h3p' size='340' side='right'caption='[[2h3p]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='2h3p' size='340' side='right'caption='[[2h3p]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2h3p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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>
<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>
</td></tr><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>
</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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ndb|1ndb]], [[1ndf|1ndf]], [[1ndi|1ndi]], [[1t7q|1t7q]], [[1t7n|1t7n]], [[1t7o|1t7o]], [[2h3u|2h3u]], [[2h3w|2h3w]]</div></td></tr>
<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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Crat ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
<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>
<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>
</table>
</table>
== Function ==
== Function ==
[[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.  
[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:16870616<ref>PMID:16870616</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2h3p" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Carnitine acetyltransferase|Carnitine acetyltransferase]]
*[[Carnitine acetyltransferase|Carnitine acetyltransferase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Hsiao, Y S]]
[[Category: Hsiao YS]]
[[Category: Jogl, G]]
[[Category: Jogl G]]
[[Category: Tong, L]]
[[Category: Tong L]]
[[Category: Carnitine acyltransferase]]
[[Category: Transferase]]

Latest revision as of 12:30, 14 February 2024

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

Structural highlights

2h3p is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2h3p, resolution 2.20Å

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