1ghj - Revision history

OCA at 11:21, 27 March 2024

OCA — Wed, 27 Mar 2024 11:21:30 GMT

←Older revision		Revision as of 11:21, 27 March 2024
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	==SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE 2-OXOGLUTARATE DEHYDROGENASE COMPLEX FROM AZOTOBACTER VINELAND II, NMR, MINIMIZED AVERAGE STRUCTURE==		==SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE 2-OXOGLUTARATE DEHYDROGENASE COMPLEX FROM AZOTOBACTER VINELAND II, NMR, MINIMIZED AVERAGE STRUCTURE==
-	<StructureSection load='1ghj' size='340' side='right'caption='[[1ghj~~]], [[NMR_Ensembles_of_Models \| 1 NMR models~~]]' scene=''>	+	<StructureSection load='1ghj' size='340' side='right'caption='[[1ghj]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ghj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_478 Atcc 478~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GHJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ghj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GHJ 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;'>[[1ghk\|1ghk]]</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~~='activity'><td class~~="~~sblockLbl~~"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] </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=1ghj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghj OCA], [https://pdbe.org/1ghj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ghj RCSB], [https://www.ebi.ac.uk/pdbsum/1ghj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ghj 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=1ghj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghj OCA], [https://pdbe.org/1ghj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ghj RCSB], [https://www.ebi.ac.uk/pdbsum/1ghj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ghj ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ODO2_AZOVI ODO2_AZOVI]] The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).	+	[https://www.uniprot.org/uniprot/ODO2_AZOVI ODO2_AZOVI] The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
	== 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=1ghj 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=1ghj ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The three-dimensional solution structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii has been determined from nuclear magnetic resonance data by using distance geometry and dynamical simulated annealing refinement. The structure determination is based on a total of 580 experimentally derived distance constraints and 65 dihedral angle constraints. The solution structure is represented by an ensemble of 25 structures with an average root-mean-square deviation between the individual structures of the ensemble and the mean coordinates of 0.71 A for backbone atoms and 1.08 A for all heavy atoms. The overall fold of the lipoyl domain is that of a beta-barrel-sandwich hybrid. It consists of two almost parallel four-stranded anti-parallel beta-sheets formed around a well-defined hydrophobic core, with a central position of the single tryptophan 21. The lipoylation site, lysine 42, is found in a beta-turn at the far end of one of the sheets, and is close in space to a solvent-exposed loop comprising residues 7 to 15. The lipoyl domain displays a remarkable internal symmetry that projects one beta-sheet onto the other beta-sheet after rotation of approximately 180 degrees about a 2-fold rotational symmetry axis. There is close structural similarity between the structure of this 2-oxoglutarate dehydrogenase complex lipoyl domain and the structures of the lipoyl domains of pyruvate dehydrogenase complexes from Bacillus stearothermophilus and Escherichia coli, and conformational differences occur primarily in a solvent-exposed loop close in space to the lipoylation site. The lipoyl domain structure is discussed in relation to the process of molecular recognition of lipoyl domains by their parent 2-oxo acid dehydrogenase.
-
-	Solution structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii.,Berg A, Vervoort J, de Kok A J Mol Biol. 1996 Aug 23;261(3):432-42. PMID:8780784<ref>PMID:8780784</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1ghj" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[2-oxoglutarate dehydrogenase 3D structures\|2-oxoglutarate dehydrogenase 3D structures]]		*[[2-oxoglutarate dehydrogenase 3D structures\|2-oxoglutarate dehydrogenase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Atcc 478]]~~	+	[[Category: Azotobacter vinelandii]]
-	~~[[Category: Dihydrolipoyllysine-residue succinyltransferase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Berg, A]]	+	[[Category: Berg A]]
-	[[Category: Kok, A De]]	+	[[Category: De Kok A]]
-	[[Category: Vervoort, J]]	+	[[Category: Vervoort J]]
-	~~[[Category: Acyltransferase]]~~	+
-	~~[[Category: Glycolysis]]~~	+
-	~~[[Category: Lipoyl]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 11:23, 28 July 2021

OCA — Wed, 28 Jul 2021 11:23:31 GMT

←Older revision		Revision as of 11:23, 28 July 2021
Line 3:		Line 3:
	<StructureSection load='1ghj' size='340' side='right'caption='[[1ghj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1ghj' size='340' side='right'caption='[[1ghj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ghj]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHJ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1GHJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ghj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GHJ FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ghk\|1ghk]]</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;'>[[1ghk\|1ghk]]</div></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_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] </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=1ghj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghj OCA], [~~http~~://pdbe.org/1ghj PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1ghj RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1ghj PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1ghj 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=1ghj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghj OCA], [https://pdbe.org/1ghj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ghj RCSB], [https://www.ebi.ac.uk/pdbsum/1ghj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ghj ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ODO2_AZOVI ODO2_AZOVI]] The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).	+	[[https://www.uniprot.org/uniprot/ODO2_AZOVI ODO2_AZOVI]] The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:25, 23 October 2019

OCA — Wed, 23 Oct 2019 08:25:23 GMT

←Older revision		Revision as of 08:25, 23 October 2019
Line 1:		Line 1:

	==SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE 2-OXOGLUTARATE DEHYDROGENASE COMPLEX FROM AZOTOBACTER VINELAND II, NMR, MINIMIZED AVERAGE STRUCTURE==		==SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE 2-OXOGLUTARATE DEHYDROGENASE COMPLEX FROM AZOTOBACTER VINELAND II, NMR, MINIMIZED AVERAGE STRUCTURE==
-	<StructureSection load='1ghj' size='340' side='right' caption='[[1ghj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>	+	<StructureSection load='1ghj' size='340' side='right'caption='[[1ghj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ghj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GHJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ghj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GHJ FirstGlance]. <br>
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gh/1ghj_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gh/1ghj_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 29:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1ghj" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1ghj" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[2-oxoglutarate dehydrogenase 3D structures\|2-oxoglutarate dehydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Atcc 478]]		[[Category: Atcc 478]]
	[[Category: Dihydrolipoyllysine-residue succinyltransferase]]		[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
		+	[[Category: Large Structures]]
	[[Category: Berg, A]]		[[Category: Berg, A]]
	[[Category: Kok, A De]]		[[Category: Kok, A De]]

OCA at 06:35, 29 November 2017

OCA — Wed, 29 Nov 2017 06:35:20 GMT

←Older revision		Revision as of 06:35, 29 November 2017
Line 1:		Line 1:
		+
	==SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE 2-OXOGLUTARATE DEHYDROGENASE COMPLEX FROM AZOTOBACTER VINELAND II, NMR, MINIMIZED AVERAGE STRUCTURE==		==SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE 2-OXOGLUTARATE DEHYDROGENASE COMPLEX FROM AZOTOBACTER VINELAND II, NMR, MINIMIZED AVERAGE STRUCTURE==
	<StructureSection load='1ghj' size='340' side='right' caption='[[1ghj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1ghj' size='340' side='right' caption='[[1ghj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
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	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ghk\|1ghk]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ghk\|1ghk]]</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_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] </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_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] </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=1ghj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghj OCA], [http://pdbe.org/1ghj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ghj RCSB], [http://www.ebi.ac.uk/pdbsum/1ghj 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=1ghj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghj OCA], [http://pdbe.org/1ghj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ghj RCSB], [http://www.ebi.ac.uk/pdbsum/1ghj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ghj ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1ghj" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1ghj" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[2-Oxoglutarate Dehydrogenase\|2-Oxoglutarate Dehydrogenase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:25, 8 February 2016

OCA — Mon, 08 Feb 2016 12:25:36 GMT

←Older revision		Revision as of 12:25, 8 February 2016
Line 17:		Line 17:
	<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=1ghj ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 11:33, 10 September 2015

OCA — Thu, 10 Sep 2015 11:33:25 GMT

←Older revision		Revision as of 11:33, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1ghj' size='340' side='right' caption='[[1ghj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1ghj' size='340' side='right' caption='[[1ghj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ghj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Azotobacter_vinelandii Azotobacter vinelandii~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GHJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ghj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GHJ FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ghk\|1ghk]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ghk\|1ghk]]</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_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] </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_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] </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=1ghj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ghj RCSB], [http://www.ebi.ac.uk/pdbsum/1ghj 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=1ghj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghj OCA], [http://pdbe.org/1ghj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ghj RCSB], [http://www.ebi.ac.uk/pdbsum/1ghj PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	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 1ghj" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Azotobacter vinelandii~~]]	+	[[Category: Atcc 478]]
	[[Category: Dihydrolipoyllysine-residue succinyltransferase]]		[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
	[[Category: Berg, A]]		[[Category: Berg, A]]

OCA at 23:18, 24 December 2014

OCA — Wed, 24 Dec 2014 23:18:20 GMT

←Older revision		Revision as of 23:18, 24 December 2014
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	<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=1ghj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ghj RCSB], [http://www.ebi.ac.uk/pdbsum/1ghj 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=1ghj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ghj RCSB], [http://www.ebi.ac.uk/pdbsum/1ghj PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ODO2_AZOVI ODO2_AZOVI]] The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 20:03, 22 December 2014

OCA — Mon, 22 Dec 2014 20:03:42 GMT

←Older revision		Revision as of 20:03, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ghj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GHJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ghj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GHJ FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ghk\|1ghk]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ghk\|1ghk]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] </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_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] </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=1ghj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ghj RCSB], [http://www.ebi.ac.uk/pdbsum/1ghj 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=1ghj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ghj RCSB], [http://www.ebi.ac.uk/pdbsum/1ghj PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 34:
	[[Category: Azotobacter vinelandii]]		[[Category: Azotobacter vinelandii]]
	[[Category: Dihydrolipoyllysine-residue succinyltransferase]]		[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
-	[[Category: Berg, A.]]	+	[[Category: Berg, A]]
-	[[Category: Kok, A De.]]	+	[[Category: Kok, A De]]
-	[[Category: Vervoort, J.]]	+	[[Category: Vervoort, J]]
	[[Category: Acyltransferase]]		[[Category: Acyltransferase]]
	[[Category: Glycolysis]]		[[Category: Glycolysis]]
	[[Category: Lipoyl]]		[[Category: Lipoyl]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 09:54, 28 September 2014

OCA — Sun, 28 Sep 2014 09:54:38 GMT

←Older revision		Revision as of 09:54, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1ghj.~~png~~\|~~left~~\|200px]]	+	==SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE 2-OXOGLUTARATE DEHYDROGENASE COMPLEX FROM AZOTOBACTER VINELAND II, NMR, MINIMIZED AVERAGE STRUCTURE==
		+	<StructureSection load='1ghj' size='340' side='right' caption='[[1ghj]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1ghj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GHJ FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1ghk\|1ghk]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_succinyltransferase Dihydrolipoyllysine-residue succinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.61 2.3.1.61] </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=1ghj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ghj RCSB], [http://www.ebi.ac.uk/pdbsum/1ghj 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/gh/1ghj_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 three-dimensional solution structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii has been determined from nuclear magnetic resonance data by using distance geometry and dynamical simulated annealing refinement. The structure determination is based on a total of 580 experimentally derived distance constraints and 65 dihedral angle constraints. The solution structure is represented by an ensemble of 25 structures with an average root-mean-square deviation between the individual structures of the ensemble and the mean coordinates of 0.71 A for backbone atoms and 1.08 A for all heavy atoms. The overall fold of the lipoyl domain is that of a beta-barrel-sandwich hybrid. It consists of two almost parallel four-stranded anti-parallel beta-sheets formed around a well-defined hydrophobic core, with a central position of the single tryptophan 21. The lipoylation site, lysine 42, is found in a beta-turn at the far end of one of the sheets, and is close in space to a solvent-exposed loop comprising residues 7 to 15. The lipoyl domain displays a remarkable internal symmetry that projects one beta-sheet onto the other beta-sheet after rotation of approximately 180 degrees about a 2-fold rotational symmetry axis. There is close structural similarity between the structure of this 2-oxoglutarate dehydrogenase complex lipoyl domain and the structures of the lipoyl domains of pyruvate dehydrogenase complexes from Bacillus stearothermophilus and Escherichia coli, and conformational differences occur primarily in a solvent-exposed loop close in space to the lipoylation site. The lipoyl domain structure is discussed in relation to the process of molecular recognition of lipoyl domains by their parent 2-oxo acid dehydrogenase.

-	~~{{STRUCTURE_1ghj\| PDB=1ghj \| SCENE= }}~~	+	Solution structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii.,Berg A, Vervoort J, de Kok A J Mol Biol. 1996 Aug 23;261(3):432-42. PMID:8780784<ref>PMID:8780784</ref>

-	~~===SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE 2-OXOGLUTARATE DEHYDROGENASE COMPLEX FROM AZOTOBACTER VINELAND II~~, ~~NMR, MINIMIZED AVERAGE STRUCTURE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_8780784}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1ghj]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]~~. ~~Full experimental information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1GHJ OCA].~~	+

	==See Also==		==See Also==
	*[[2-Oxoglutarate Dehydrogenase\|2-Oxoglutarate Dehydrogenase]]		*[[2-Oxoglutarate Dehydrogenase\|2-Oxoglutarate Dehydrogenase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:008780784<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Azotobacter vinelandii]]		[[Category: Azotobacter vinelandii]]
	[[Category: Dihydrolipoyllysine-residue succinyltransferase]]		[[Category: Dihydrolipoyllysine-residue succinyltransferase]]

OCA at 10:07, 20 October 2012

OCA — Sat, 20 Oct 2012 10:07:53 GMT

←Older revision		Revision as of 10:07, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1ghj]] is a 1 chain structure ~~of [[2-Oxoglutarate Dehydrogenase]]~~ with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHJ OCA].	+	[[1ghj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHJ OCA].

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