1lab - Revision history

OCA at 08:07, 3 April 2024

OCA — Wed, 03 Apr 2024 08:07:58 GMT

←Older revision		Revision as of 08:07, 3 April 2024
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	==THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX==		==THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX==
-	<StructureSection load='1lab' size='340' side='right'caption='[[1lab~~]], [[NMR_Ensembles_of_Models \| 11 NMR models~~]]' scene=''>	+	<StructureSection load='1lab' size='340' side='right'caption='[[1lab]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1lab]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Atcc_12980 Atcc 12980~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1LAB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1lab]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LAB FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1lac\|1lac]]</div></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BACILLUS STEAROTHERMOPHILUS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</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=1lab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lab OCA], [https://pdbe.org/1lab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lab RCSB], [https://www.ebi.ac.uk/pdbsum/1lab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lab ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </span></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=1lab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lab OCA], [~~http~~://pdbe.org/1lab PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1lab RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1lab PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1lab ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ODP2_GEOSE ODP2_GEOSE]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).	+	[https://www.uniprot.org/uniprot/ODP2_GEOSE ODP2_GEOSE] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 21:		Line 19:
	</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=1lab 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=1lab ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The structure of the lipoyl domain from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus has been determined by means of nuclear magnetic resonance spectroscopy. A total of 452 nuclear Overhauser effect distance constraints and 76 dihedral angle restraints were employed as the input for the structure calculations, which were performed using a hybrid distance geometry-simulated annealing strategy and the programs DISGEO and X-PLOR. The overall structure of the lipoyl domain (residues 1 to 79 of the dihydrolipoamide acetyltransferase polypeptide chain) is that of a flattened eight-stranded beta-barrel folded around a core of well-defined hydrophobic residues. The lipoylation site, lysine 42, is located in the middle of a beta-turn, and the N and C-terminal residues of the domain are close together in adjacent beta-strands at the opposite end of the molecule. The polypeptide backbone exhibits a 2-fold axis of quasi-symmetry, with the C alpha atoms of residues 15 to 39 and 52 to 76 being almost superimposable on those of residues 52 to 76 and 15 to 39, respectively (root-mean-square deviation = 1.48 A). The amino acid residues at key positions in the structure are conserved among all the reported primary structures of lipoyl domains, suggesting that the domains all fold in a similar way.
-
-	Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex.,Dardel F, Davis AL, Laue ED, Perham RN J Mol Biol. 1993 Feb 20;229(4):1037-48. PMID:8445635<ref>PMID:8445635</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1lab" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[Dihydrolipoamide acetyltransferase\|Dihydrolipoamide acetyltransferase]]	+	*[[Dihydrolipoamide acetyltransferase 3D structures\|Dihydrolipoamide acetyltransferase 3D structures]]
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Atcc 12980]]~~	+	[[Category: Geobacillus stearothermophilus]]
-	~~[[Category: Dihydrolipoyllysine-residue acetyltransferase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Dardel, F]]	+	[[Category: Dardel F]]
-	[[Category: Davis~~, A L~~]]	+	[[Category: Davis AL]]
-	[[Category: Laue~~, E D~~]]	+	[[Category: Laue ED]]
-	[[Category: Perham~~, R N~~]]	+	[[Category: Perham RN]]

OCA at 07:57, 25 November 2020

OCA — Wed, 25 Nov 2020 07:57:07 GMT

←Older revision		Revision as of 07:57, 25 November 2020
Line 1:		Line 1:

	==THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX==		==THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX==
-	<StructureSection load='1lab' size='340' side='right' caption='[[1lab]], [[NMR_Ensembles_of_Models \| 11 NMR models]]' scene=''>	+	<StructureSection load='1lab' size='340' side='right'caption='[[1lab]], [[NMR_Ensembles_of_Models \| 11 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1lab]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1LAB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1lab]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1LAB FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lac\|1lac]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1lac\|1lac]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BACILLUS STEAROTHERMOPHILUS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BACILLUS STEAROTHERMOPHILUS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </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=1lab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lab OCA], [http://pdbe.org/1lab PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lab RCSB], [http://www.ebi.ac.uk/pdbsum/1lab PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lab ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1lab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lab OCA], [http://pdbe.org/1lab PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lab RCSB], [http://www.ebi.ac.uk/pdbsum/1lab PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lab ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/la/1lab_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/la/1lab_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>
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1lab" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1lab" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Dihydrolipoamide acetyltransferase\|Dihydrolipoamide acetyltransferase]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 39:
	[[Category: Atcc 12980]]		[[Category: Atcc 12980]]
	[[Category: Dihydrolipoyllysine-residue acetyltransferase]]		[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
		+	[[Category: Large Structures]]
	[[Category: Dardel, F]]		[[Category: Dardel, F]]
	[[Category: Davis, A L]]		[[Category: Davis, A L]]
	[[Category: Laue, E D]]		[[Category: Laue, E D]]
	[[Category: Perham, R N]]		[[Category: Perham, R N]]

OCA at 06:43, 29 November 2017

OCA — Wed, 29 Nov 2017 06:43:50 GMT

←Older revision		Revision as of 06:43, 29 November 2017
Line 1:		Line 1:
		+
	==THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX==		==THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX==
	<StructureSection load='1lab' size='340' side='right' caption='[[1lab]], [[NMR_Ensembles_of_Models \| 11 NMR models]]' scene=''>		<StructureSection load='1lab' size='340' side='right' caption='[[1lab]], [[NMR_Ensembles_of_Models \| 11 NMR models]]' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BACILLUS STEAROTHERMOPHILUS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BACILLUS STEAROTHERMOPHILUS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </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=1lab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lab OCA], [http://pdbe.org/1lab PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lab RCSB], [http://www.ebi.ac.uk/pdbsum/1lab 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=1lab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lab OCA], [http://pdbe.org/1lab PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lab RCSB], [http://www.ebi.ac.uk/pdbsum/1lab PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lab ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1lab" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1lab" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Dihydrolipoamide acetyltransferase\|Dihydrolipoamide acetyltransferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 01:26, 9 February 2016

OCA — Tue, 09 Feb 2016 01:26:02 GMT

←Older revision		Revision as of 01:26, 9 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=1lab ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 17:16, 10 September 2015

OCA — Thu, 10 Sep 2015 17:16:06 GMT

←Older revision		Revision as of 17:16, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1lab' size='340' side='right' caption='[[1lab]], [[NMR_Ensembles_of_Models \| 11 NMR models]]' scene=''>		<StructureSection load='1lab' size='340' side='right' caption='[[1lab]], [[NMR_Ensembles_of_Models \| 11 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1lab]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Geobacillus_stearothermophilus Geobacillus stearothermophilus~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LAB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1lab]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LAB FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lac\|1lac]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lac\|1lac]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BACILLUS STEAROTHERMOPHILUS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ~~Geobacillus stearothermophilus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BACILLUS STEAROTHERMOPHILUS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </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=1lab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lab OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lab RCSB], [http://www.ebi.ac.uk/pdbsum/1lab 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=1lab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lab OCA], [http://pdbe.org/1lab PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lab RCSB], [http://www.ebi.ac.uk/pdbsum/1lab PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~ODP2_BACST ODP2_BACST~~]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).	+	[[http://www.uniprot.org/uniprot/ODP2_GEOSE ODP2_GEOSE]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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 1lab" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Atcc 12980]]
	[[Category: Dihydrolipoyllysine-residue acetyltransferase]]		[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
-	[[Category: Geobacillus stearothermophilus]]
	[[Category: Dardel, F]]		[[Category: Dardel, F]]
	[[Category: Davis, A L]]		[[Category: Davis, A L]]
	[[Category: Laue, E D]]		[[Category: Laue, E D]]
	[[Category: Perham, R N]]		[[Category: Perham, R N]]

OCA at 03:28, 25 December 2014

OCA — Thu, 25 Dec 2014 03:28:59 GMT

←Older revision		Revision as of 03:28, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1lab]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LAB FirstGlance]. <br>		<table><tr><td colspan='2'>[[1lab]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LAB FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lac\|1lac]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lac\|1lac]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BACILLUS STEAROTHERMOPHILUS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BACILLUS STEAROTHERMOPHILUS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus])</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </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=1lab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lab OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lab RCSB], [http://www.ebi.ac.uk/pdbsum/1lab 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=1lab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lab OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lab RCSB], [http://www.ebi.ac.uk/pdbsum/1lab PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ODP2_BACST ODP2_BACST]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 37:
	[[Category: Dihydrolipoyllysine-residue acetyltransferase]]		[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
	[[Category: Geobacillus stearothermophilus]]		[[Category: Geobacillus stearothermophilus]]
-	[[Category: Dardel, F.]]	+	[[Category: Dardel, F]]
-	[[Category: Davis, A L.]]	+	[[Category: Davis, A L]]
-	[[Category: Laue, E D.]]	+	[[Category: Laue, E D]]
-	[[Category: Perham, R N.]]	+	[[Category: Perham, R N]]

OCA at 13:57, 28 September 2014

OCA — Sun, 28 Sep 2014 13:57:58 GMT

←Older revision		Revision as of 13:57, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1lab.~~png~~\|~~left~~\|200px]]	+	==THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX==
		+	<StructureSection load='1lab' size='340' side='right' caption='[[1lab]], [[NMR_Ensembles_of_Models \| 11 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1lab]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LAB FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lac\|1lac]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BACILLUS STEAROTHERMOPHILUS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </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=1lab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lab OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lab RCSB], [http://www.ebi.ac.uk/pdbsum/1lab 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/la/1lab_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 ==
		+	The structure of the lipoyl domain from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus has been determined by means of nuclear magnetic resonance spectroscopy. A total of 452 nuclear Overhauser effect distance constraints and 76 dihedral angle restraints were employed as the input for the structure calculations, which were performed using a hybrid distance geometry-simulated annealing strategy and the programs DISGEO and X-PLOR. The overall structure of the lipoyl domain (residues 1 to 79 of the dihydrolipoamide acetyltransferase polypeptide chain) is that of a flattened eight-stranded beta-barrel folded around a core of well-defined hydrophobic residues. The lipoylation site, lysine 42, is located in the middle of a beta-turn, and the N and C-terminal residues of the domain are close together in adjacent beta-strands at the opposite end of the molecule. The polypeptide backbone exhibits a 2-fold axis of quasi-symmetry, with the C alpha atoms of residues 15 to 39 and 52 to 76 being almost superimposable on those of residues 52 to 76 and 15 to 39, respectively (root-mean-square deviation = 1.48 A). The amino acid residues at key positions in the structure are conserved among all the reported primary structures of lipoyl domains, suggesting that the domains all fold in a similar way.

-	~~{{STRUCTURE_1lab\| PDB=1lab \| SCENE= }}~~	+	Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex.,Dardel F, Davis AL, Laue ED, Perham RN J Mol Biol. 1993 Feb 20;229(4):1037-48. PMID:8445635<ref>PMID:8445635</ref>

-	~~===THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_8445635}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1lab]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]~~. ~~Full experimental information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA].~~	+

	==See Also==		==See Also==
	*[[Dihydrolipoamide acetyltransferase\|Dihydrolipoamide acetyltransferase]]		*[[Dihydrolipoamide acetyltransferase\|Dihydrolipoamide acetyltransferase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:008445635<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Dihydrolipoyllysine-residue acetyltransferase]]		[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
	[[Category: Geobacillus stearothermophilus]]		[[Category: Geobacillus stearothermophilus]]

OCA at 12:09, 20 October 2012

OCA — Sat, 20 Oct 2012 12:09:41 GMT

←Older revision		Revision as of 12:09, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1lab]] is a 1 chain structure ~~of [[Dihydrolipoamide acetyltransferase]]~~ with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA].	+	[[1lab]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA].

	==See Also==		==See Also==

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

OCA — Thu, 26 Jul 2012 07:48:38 GMT

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

←Older revision

Revision as of 07:48, 26 July 2012

OCA at 07:48, 26 July 2012

OCA — Thu, 26 Jul 2012 07:48:36 GMT

←Older revision		Revision as of 07:48, 26 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1lab.png\|left\|200px]]		[[Image:1lab.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1lab", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1lab\| PDB=1lab \| SCENE= }}		{{STRUCTURE_1lab\| PDB=1lab \| SCENE= }}

	===THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX===		===THREE-DIMENSIONAL STRUCTURE OF THE LIPOYL DOMAIN FROM BACILLUS STEAROTHERMOPHILUS PYRUVATE DEHYDROGENASE MULTIENZYME COMPLEX===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_8445635}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 8445635 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_8445635}}		{{ABSTRACT_PUBMED_8445635}}

	==About this Structure==		==About this Structure==
-	~~1LAB~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA].	+	[[1lab]] is a 1 chain structure of [[Dihydrolipoamide acetyltransferase]] with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAB OCA].
		+
		+	==See Also==
		+	*[[Dihydrolipoamide acetyltransferase\|Dihydrolipoamide acetyltransferase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~8445635~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:008445635</ref><references group="xtra"/>
	[[Category: Dihydrolipoyllysine-residue acetyltransferase]]		[[Category: Dihydrolipoyllysine-residue acetyltransferase]]
	[[Category: Geobacillus stearothermophilus]]		[[Category: Geobacillus stearothermophilus]]
Line 30:		Line 21:
	[[Category: Laue, E D.]]		[[Category: Laue, E D.]]
	[[Category: Perham, R N.]]		[[Category: Perham, R N.]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 05:20:19 2009''