1t7q - Revision history

OCA at 08:37, 14 February 2024

OCA — Wed, 14 Feb 2024 08:37:16 GMT

←Older revision		Revision as of 08:37, 14 February 2024
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	<StructureSection load='1t7q' size='340' side='right'caption='[[1t7q]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1t7q' size='340' side='right'caption='[[1t7q]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1t7q]] 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=1T7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T7Q FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1t7q]] 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=1T7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T7Q 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=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:~~1~~,2-ETHANEDIOL'>EDO</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]] 1.8Å</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]], [[1t7n\|1t7n]], [[1t7o\|1t7o]]~~</~~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=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[https~~:~~//en.wikipedia.org/wiki/Carnitine_O-acetyltransferase Carnitine O-acetyltransferase]~~, ~~with EC number [https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=2.3.1.7 2.3.1.7]~~ </~~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=1t7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7q OCA], [https://pdbe.org/1t7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t7q RCSB], [https://www.ebi.ac.uk/pdbsum/1t7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t7q 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=1t7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7q OCA], [https://pdbe.org/1t7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t7q RCSB], [https://www.ebi.ac.uk/pdbsum/1t7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t7q 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=1t7q 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=1t7q ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Carnitine acyltransferases catalyze the 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, and are attractive targets for drug discovery against diabetes and obesity. These enzymes are classified based on their substrate selectivity for short-chain, medium-chain, or long-chain fatty acids. Structural information on carnitine acetyltransferase suggests that residues Met-564 and Phe-565 may be important determinants of substrate selectivity with the side chain of Met-564 located in the putative binding pocket for acyl groups. Both residues are replaced by glycine in carnitine palmitoyltransferases. To assess the functional relevance of this structural observation, we have replaced these two residues with small amino acids by mutagenesis, characterized the substrate preference of the mutants, and determined the crystal structures of two of these mutants. Kinetic studies confirm that the M564G or M564A mutation is sufficient to increase the activity of the enzyme toward medium-chain substrates with hexanoyl-CoA being the preferred substrate for the M564G mutant. The crystal structures of the M564G mutant, both alone and in complex with carnitine, reveal a deep binding pocket that can accommodate the larger acyl group. We have determined the crystal structure of the F565A mutant in a ternary complex with both the carnitine and CoA substrates at a 1.8-A resolution. The F565A mutation has minor effects on the structure or the substrate preference of the enzyme.
-
-	Structural and biochemical studies of the substrate selectivity of carnitine acetyltransferase.,Hsiao YS, Jogl G, Tong L J Biol Chem. 2004 Jul 23;279(30):31584-9. Epub 2004 May 21. PMID:15155726<ref>PMID:15155726</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1t7q" style="background-color:#fffaf0;"></div>

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

OCA at 09:23, 29 September 2021

OCA — Wed, 29 Sep 2021 09:23:53 GMT

←Older revision		Revision as of 09:23, 29 September 2021
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	<StructureSection load='1t7q' size='340' side='right'caption='[[1t7q]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1t7q' size='340' side='right'caption='[[1t7q]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1t7q]] is a 2 chain structure with sequence from [~~http~~://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=1T7Q OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1T7Q FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1t7q]] 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=1T7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T7Q FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=152:CARNITINE'>152</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>	+	</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=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ndb\|1ndb]], [[1ndf\|1ndf]], [[1ndi\|1ndi]], [[1t7n\|1t7n]], [[1t7o\|1t7o]]</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]], [[1t7n\|1t7n]], [[1t7o\|1t7o]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Carnitine_O-acetyltransferase Carnitine O-acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.7 2.3.1.7] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1t7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7q OCA], [~~http~~://pdbe.org/1t7q PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1t7q RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1t7q PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1t7q 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=1t7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7q OCA], [https://pdbe.org/1t7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t7q RCSB], [https://www.ebi.ac.uk/pdbsum/1t7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t7q ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://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]]

OCA at 13:54, 18 December 2019

OCA — Wed, 18 Dec 2019 13:54:44 GMT

←Older revision		Revision as of 13:54, 18 December 2019
Line 1:		Line 1:

	==Crystal structure of the F565A mutant of murine carnitine acetyltransferase in complex with carnitine and CoA==		==Crystal structure of the F565A mutant of murine carnitine acetyltransferase in complex with carnitine and CoA==
-	<StructureSection load='1t7q' size='340' side='right' caption='[[1t7q]], [[Resolution\|resolution]] 1.80Å' scene=''>	+	<StructureSection load='1t7q' size='340' side='right'caption='[[1t7q]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1t7q]] is a 2 chain structure with sequence from [http://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=1T7Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T7Q FirstGlance]. <br>		<table><tr><td colspan='2'>[[1t7q]] is a 2 chain structure with sequence from [http://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=1T7Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T7Q FirstGlance]. <br>
Line 38:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Carnitine O-acetyltransferase]]		[[Category: Carnitine O-acetyltransferase]]
		+	[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Hsiao, Y S]]		[[Category: Hsiao, Y S]]

OCA at 07:39, 14 March 2018

OCA — Wed, 14 Mar 2018 07:39:04 GMT

←Older revision		Revision as of 07:39, 14 March 2018
Line 1:		Line 1:
		+
	==Crystal structure of the F565A mutant of murine carnitine acetyltransferase in complex with carnitine and CoA==		==Crystal structure of the F565A mutant of murine carnitine acetyltransferase in complex with carnitine and CoA==
	<StructureSection load='1t7q' size='340' side='right' caption='[[1t7q]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1t7q' size='340' side='right' caption='[[1t7q]], [[Resolution\|resolution]] 1.80Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ndb\|1ndb]], [[1ndf\|1ndf]], [[1ndi\|1ndi]], [[1t7n\|1t7n]], [[1t7o\|1t7o]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ndb\|1ndb]], [[1ndf\|1ndf]], [[1ndi\|1ndi]], [[1t7n\|1t7n]], [[1t7o\|1t7o]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7q OCA], [http://pdbe.org/1t7q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t7q RCSB], [http://www.ebi.ac.uk/pdbsum/1t7q PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7q OCA], [http://pdbe.org/1t7q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t7q RCSB], [http://www.ebi.ac.uk/pdbsum/1t7q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t7q ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t7/1t7q_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t7/1t7q_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 02:24, 7 February 2016

OCA — Sun, 07 Feb 2016 02:24:16 GMT

←Older revision		Revision as of 02:24, 7 February 2016
Line 18:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</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/~~chain_selection~~.php?pdb_ID=~~2ata~~ 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=1t7q ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 20:46, 9 September 2015

OCA — Wed, 09 Sep 2015 20:46:47 GMT

←Older revision		Revision as of 20:46, 9 September 2015
Line 2:		Line 2:
	<StructureSection load='1t7q' size='340' side='right' caption='[[1t7q]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='1t7q' size='340' side='right' caption='[[1t7q]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1t7q]] is a 2 chain structure with 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=1T7Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T7Q FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1t7q]] is a 2 chain structure with sequence from [http://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=1T7Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T7Q FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=152:CARNITINE'>152</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=152:CARNITINE'>152</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ndb\|1ndb]], [[1ndf\|1ndf]], [[1ndi\|1ndi]], [[1t7n\|1t7n]], [[1t7o\|1t7o]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ndb\|1ndb]], [[1ndf\|1ndf]], [[1ndi\|1ndi]], [[1t7n\|1t7n]], [[1t7o\|1t7o]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1t7q RCSB], [http://www.ebi.ac.uk/pdbsum/1t7q PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7q OCA], [http://pdbe.org/1t7q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t7q RCSB], [http://www.ebi.ac.uk/pdbsum/1t7q PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1t7q" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Carnitine O-acetyltransferase]]		[[Category: Carnitine O-acetyltransferase]]
-	[[Category: ~~Mus musculus~~]]	+	[[Category: Lk3 transgenic mice]]
	[[Category: Hsiao, Y S]]		[[Category: Hsiao, Y S]]
	[[Category: Jogl, G]]		[[Category: Jogl, G]]
	[[Category: Tong, L]]		[[Category: Tong, L]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 07:04, 24 December 2014

OCA — Wed, 24 Dec 2014 07:04:37 GMT

←Older revision		Revision as of 07:04, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1t7q]] is a 2 chain structure with 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=1T7Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T7Q FirstGlance]. <br>		<table><tr><td colspan='2'>[[1t7q]] is a 2 chain structure with 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=1T7Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T7Q FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=152:CARNITINE'>152</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=152:CARNITINE'>152</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ndb\|1ndb]], [[1ndf\|1ndf]], [[1ndi\|1ndi]], [[1t7n\|1t7n]], [[1t7o\|1t7o]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ndb\|1ndb]], [[1ndf\|1ndf]], [[1ndi\|1ndi]], [[1t7n\|1t7n]], [[1t7o\|1t7o]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1t7q RCSB], [http://www.ebi.ac.uk/pdbsum/1t7q PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1t7q RCSB], [http://www.ebi.ac.uk/pdbsum/1t7q PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://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]]
Line 35:		Line 37:
	[[Category: Carnitine O-acetyltransferase]]		[[Category: Carnitine O-acetyltransferase]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Hsiao, Y S.]]	+	[[Category: Hsiao, Y S]]
-	[[Category: Jogl, G.]]	+	[[Category: Jogl, G]]
-	[[Category: Tong, L.]]	+	[[Category: Tong, L]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 18:29, 29 September 2014

OCA — Mon, 29 Sep 2014 18:29:44 GMT

←Older revision		Revision as of 18:29, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1t7q\| PDB=1t7q \| SCENE= }}~~	+	==Crystal structure of the F565A mutant of murine carnitine acetyltransferase in complex with carnitine and CoA==
-	===Crystal structure of the F565A mutant of murine carnitine acetyltransferase in complex with carnitine and CoA===	+	<StructureSection load='1t7q' size='340' side='right' caption='[[1t7q]], [[Resolution\|resolution]] 1.80Å' scene=''>
-	~~{{ABSTRACT_PUBMED_15155726}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1t7q]] is a 2 chain structure with 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=1T7Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T7Q FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=152:CARNITINE'>152</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ndb\|1ndb]], [[1ndf\|1ndf]], [[1ndi\|1ndi]], [[1t7n\|1t7n]], [[1t7o\|1t7o]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1t7q RCSB], [http://www.ebi.ac.uk/pdbsum/1t7q PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t7/1t7q_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</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/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Carnitine acyltransferases catalyze the 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, and are attractive targets for drug discovery against diabetes and obesity. These enzymes are classified based on their substrate selectivity for short-chain, medium-chain, or long-chain fatty acids. Structural information on carnitine acetyltransferase suggests that residues Met-564 and Phe-565 may be important determinants of substrate selectivity with the side chain of Met-564 located in the putative binding pocket for acyl groups. Both residues are replaced by glycine in carnitine palmitoyltransferases. To assess the functional relevance of this structural observation, we have replaced these two residues with small amino acids by mutagenesis, characterized the substrate preference of the mutants, and determined the crystal structures of two of these mutants. Kinetic studies confirm that the M564G or M564A mutation is sufficient to increase the activity of the enzyme toward medium-chain substrates with hexanoyl-CoA being the preferred substrate for the M564G mutant. The crystal structures of the M564G mutant, both alone and in complex with carnitine, reveal a deep binding pocket that can accommodate the larger acyl group. We have determined the crystal structure of the F565A mutant in a ternary complex with both the carnitine and CoA substrates at a 1.8-A resolution. The F565A mutation has minor effects on the structure or the substrate preference of the enzyme.

-	~~==About this Structure==~~	+	Structural and biochemical studies of the substrate selectivity of carnitine acetyltransferase.,Hsiao YS, Jogl G, Tong L J Biol Chem. 2004 Jul 23;279(30):31584-9. Epub 2004 May 21. PMID:15155726<ref>PMID:15155726</ref>
-	~~[[1t7q]] is a 2 chain structure with 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=1T7Q OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Carnitine acetyltransferase\|Carnitine acetyltransferase]]		*[[Carnitine acetyltransferase\|Carnitine acetyltransferase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:015155726<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Carnitine O-acetyltransferase]]		[[Category: Carnitine O-acetyltransferase]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]

OCA at 09:16, 11 March 2013

OCA — Mon, 11 Mar 2013 09:16:58 GMT

←Older revision		Revision as of 09:16, 11 March 2013
Line 1:		Line 1:
-	[[Image:1t7q.png\|left\|200px]]
-
	{{STRUCTURE_1t7q\| PDB=1t7q \| SCENE= }}		{{STRUCTURE_1t7q\| PDB=1t7q \| SCENE= }}
-
	===Crystal structure of the F565A mutant of murine carnitine acetyltransferase in complex with carnitine and CoA===		===Crystal structure of the F565A mutant of murine carnitine acetyltransferase in complex with carnitine and CoA===
-
	{{ABSTRACT_PUBMED_15155726}}		{{ABSTRACT_PUBMED_15155726}}

OCA: Protected "1t7q" [edit=sysop:move=sysop]

OCA — Sat, 05 Jan 2013 11:08:07 GMT

Protected "1t7q" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:08, 5 January 2013