1c4t - Revision history

OCA at 05:47, 9 August 2023

2023-08-09T05:47:52Z

←Older revision		Revision as of 05:47, 9 August 2023
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	<StructureSection load='1c4t' size='340' side='right'caption='[[1c4t]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='1c4t' size='340' side='right'caption='[[1c4t]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1c4t]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C4T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1c4t]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C4T FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3Å</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='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1c4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4t OCA], [https://pdbe.org/1c4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c4t RCSB], [https://www.ebi.ac.uk/pdbsum/1c4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c4t 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=1c4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4t OCA], [https://pdbe.org/1c4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c4t RCSB], [https://www.ebi.ac.uk/pdbsum/1c4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c4t ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ODO2_ECOLI ODO2_ECOLI]] The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).	+	[https://www.uniprot.org/uniprot/ODO2_ECOLI ODO2_ECOLI] The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three 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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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Carroll, D]]	+	[[Category: Carroll D]]
-	[[Category: Ernst~~, S R~~]]	+	[[Category: Ernst SR]]
-	[[Category: Hackert~~, M L~~]]	+	[[Category: Hackert ML]]
-	[[Category: Knapp~~, J E~~]]	+	[[Category: Knapp JE]]
-	[[Category: Lawson~~, J E~~]]	+	[[Category: Lawson JE]]
-	[[Category: Reed~~, L J]]~~	+	[[Category: Reed LJ]]
-	~~[[Category: Acyltransferase]]~~	+
-	~~[[Category: Ketoglutarate dehydrogenase multienzyme complex]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 15:14, 3 March 2021

2021-03-03T15:14:06Z

←Older revision		Revision as of 15:14, 3 March 2021
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	<StructureSection load='1c4t' size='340' side='right'caption='[[1c4t]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='1c4t' size='340' side='right'caption='[[1c4t]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1c4t]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4T OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1C4T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1c4t]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C4T FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1c4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4t OCA], [~~http~~://pdbe.org/1c4t PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1c4t RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1c4t PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1c4t 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=1c4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4t OCA], [https://pdbe.org/1c4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c4t RCSB], [https://www.ebi.ac.uk/pdbsum/1c4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c4t ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ODO2_ECOLI ODO2_ECOLI]] The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).	+	[[https://www.uniprot.org/uniprot/ODO2_ECOLI ODO2_ECOLI]] The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three 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 07:32, 29 May 2019

2019-05-29T07:32:43Z

←Older revision		Revision as of 07:32, 29 May 2019
Line 1:		Line 1:

	==CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE==		==CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE==
-	<StructureSection load='1c4t' size='340' side='right' caption='[[1c4t]], [[Resolution\|resolution]] 3.00Å' scene=''>	+	<StructureSection load='1c4t' size='340' side='right'caption='[[1c4t]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1c4t]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C4T FirstGlance]. <br>		<table><tr><td colspan='2'>[[1c4t]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C4T 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/c4/1c4t_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c4/1c4t_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 31:		Line 31:

	==See Also==		==See Also==
-	*[[2-~~Oxoglutarate Dehydrogenase~~\|2-~~Oxoglutarate Dehydrogenase~~]]	+	*[[2-oxoglutarate dehydrogenase 3D structures\|2-oxoglutarate dehydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 37:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Dihydrolipoyllysine-residue succinyltransferase]]		[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
		+	[[Category: Large Structures]]
	[[Category: Carroll, D]]		[[Category: Carroll, D]]
	[[Category: Ernst, S R]]		[[Category: Ernst, S R]]

OCA at 11:16, 24 August 2017

2017-08-24T11:16:25Z

←Older revision		Revision as of 11:16, 24 August 2017
Line 1:		Line 1:
		+
	==CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE==		==CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE==
	<StructureSection load='1c4t' size='340' side='right' caption='[[1c4t]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='1c4t' size='340' side='right' caption='[[1c4t]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1c4t]] is a 3 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Ecobd Ecobd]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C4T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1c4t]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C4T FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SUCB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=469008 ECOBD])</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=1c4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4t OCA], [http://pdbe.org/1c4t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c4t RCSB], [http://www.ebi.ac.uk/pdbsum/1c4t 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=1c4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4t OCA], [http://pdbe.org/1c4t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c4t RCSB], [http://www.ebi.ac.uk/pdbsum/1c4t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1c4t ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	<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=1c4t ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 37:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Dihydrolipoyllysine-residue succinyltransferase]]		[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
-	[[Category: Ecobd]]
	[[Category: Carroll, D]]		[[Category: Carroll, D]]
	[[Category: Ernst, S R]]		[[Category: Ernst, S R]]

OCA at 15:33, 11 September 2015

2015-09-11T15:33:48Z

←Older revision		Revision as of 15:33, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1c4t' size='340' side='right' caption='[[1c4t]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='1c4t' size='340' side='right' caption='[[1c4t]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1c4t]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli_bl21(de3) Escherichia coli bl21(de3)~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C4T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1c4t]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecobd Ecobd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C4T FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SUCB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=469008 ~~Escherichia coli BL21(DE3)~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SUCB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=469008 ECOBD])</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=1c4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c4t RCSB], [http://www.ebi.ac.uk/pdbsum/1c4t 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=1c4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4t OCA], [http://pdbe.org/1c4t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c4t RCSB], [http://www.ebi.ac.uk/pdbsum/1c4t 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 1c4t" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Dihydrolipoyllysine-residue succinyltransferase]]		[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
		+	[[Category: Ecobd]]
	[[Category: Carroll, D]]		[[Category: Carroll, D]]
	[[Category: Ernst, S R]]		[[Category: Ernst, S R]]

OCA at 18:27, 25 December 2014

2014-12-25T18:27:11Z

←Older revision		Revision as of 18:27, 25 December 2014
Line 8:		Line 8:
	<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=1c4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c4t RCSB], [http://www.ebi.ac.uk/pdbsum/1c4t 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=1c4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c4t RCSB], [http://www.ebi.ac.uk/pdbsum/1c4t PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ODO2_ECOLI ODO2_ECOLI]] The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three 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 11:11, 22 December 2014

2014-12-22T11:11:20Z

←Older revision		Revision as of 11:11, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1c4t]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_bl21(de3) Escherichia coli bl21(de3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C4T FirstGlance]. <br>		<table><tr><td colspan='2'>[[1c4t]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_bl21(de3) Escherichia coli bl21(de3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C4T FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SUCB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=469008 Escherichia coli BL21(DE3)])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SUCB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=469008 Escherichia coli BL21(DE3)])</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=1c4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c4t RCSB], [http://www.ebi.ac.uk/pdbsum/1c4t 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=1c4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c4t RCSB], [http://www.ebi.ac.uk/pdbsum/1c4t 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:
	</StructureSection>		</StructureSection>
	[[Category: Dihydrolipoyllysine-residue succinyltransferase]]		[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
-	[[Category: Carroll, D.]]	+	[[Category: Carroll, D]]
-	[[Category: Ernst, S R.]]	+	[[Category: Ernst, S R]]
-	[[Category: Hackert, M L.]]	+	[[Category: Hackert, M L]]
-	[[Category: Knapp, J E.]]	+	[[Category: Knapp, J E]]
-	[[Category: Lawson, J E.]]	+	[[Category: Lawson, J E]]
-	[[Category: Reed, L J.]]	+	[[Category: Reed, L J]]
	[[Category: Acyltransferase]]		[[Category: Acyltransferase]]
	[[Category: Ketoglutarate dehydrogenase multienzyme complex]]		[[Category: Ketoglutarate dehydrogenase multienzyme complex]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 17:07, 20 August 2014

2014-08-20T17:07:10Z

←Older revision		Revision as of 17:07, 20 August 2014
Line 1:		Line 1:
-	[[~~Image:~~1c4t.~~png~~\|~~left~~\|200px]]	+	==CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE==
		+	<StructureSection load='1c4t' size='340' side='right' caption='[[1c4t]], [[Resolution\|resolution]] 3.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1c4t]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_bl21(de3) Escherichia coli bl21(de3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C4T FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SUCB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=469008 Escherichia coli BL21(DE3)])</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=1c4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c4t RCSB], [http://www.ebi.ac.uk/pdbsum/1c4t 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/c4/1c4t_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 dihydrolipoamide succinyltransferase (E2o) component of the alpha-ketoglutarate dehydrogenase complex catalyzes the transfer of a succinyl group from the S-succinyldihydrolipoyl moiety to coenzyme A. E2o is normally a 24-mer, but is found as a trimer when E2o is expressed with a C-terminal [His]6 tag. The crystal structure of the trimeric form of the catalytic domain (CD) of the Escherichia coli E2o has been solved to 3.0 A resolution using the Molecular Replacement method. The refined model contains an intact trimer in the asymmetric unit and has an R-factor of 0.257 (Rfree = 0.286) for 18,699 reflections between 10.0 and 3.0 A resolution. The core of tE2oCD (residues 187-396) superimposes onto that of the cubic E2oCD with an RMS difference of 0.4 A for all main-chain atoms. The C-terminal end of tE2oCD (residues 397-404) rotates by an average of 37 degrees compared to cubic E2oCD, disrupting the normal twofold interface. Despite the alteration of quaternary structure, the active site of tE2oCD shows no significant differences from that of the cubic E2oCD, although several side chains in the active site are more ordered in the trimeric form of E2oCD. Analysis of the available sequence data suggests that the majority of E2 components have active sites that resemble that of E. coli E2oCD. The remaining E2 components can be divided into three groups based on active-site sequence similarity. Analysis of the surface properties of both crystal forms of E. coli E2oCD suggests key residues that may be involved in the protein-protein contacts that occur between the catalytic and lipoyl domains of E2o.

-	~~{{STRUCTURE_1c4t\| PDB=1c4t \| SCENE= }}~~	+	Expression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferase.,Knapp JE, Carroll D, Lawson JE, Ernst SR, Reed LJ, Hackert ML Protein Sci. 2000 Jan;9(1):37-48. PMID:10739245<ref>PMID:10739245</ref>

-	~~===CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_10739245}}~~	+	==See Also==
-		+	*[[2-Oxoglutarate Dehydrogenase\|2-Oxoglutarate Dehydrogenase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1c4t~~]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_bl21(de3) Escherichia coli bl21(de3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4T OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:010739245<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Dihydrolipoyllysine-residue succinyltransferase]]		[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
	[[Category: Carroll, D.]]		[[Category: Carroll, D.]]

OCA: Protected "1c4t" [edit=sysop:move=sysop]

2012-10-21T20:43:39Z

Protected "1c4t" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:43, 21 October 2012

OCA at 20:43, 21 October 2012

2012-10-21T20:43:33Z

←Older revision		Revision as of 20:43, 21 October 2012
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-	{{Seed}}
	[[Image:1c4t.png\|left\|200px]]		[[Image:1c4t.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_1c4t\| PDB=1c4t \| SCENE= }}		{{STRUCTURE_1c4t\| PDB=1c4t \| SCENE= }}

	===CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE===		===CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_10739245}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 10739245 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_10739245}}		{{ABSTRACT_PUBMED_10739245}}

	==About this Structure==		==About this Structure==
-	~~1C4T~~ is a 3 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/~~Escherichia_coli~~ Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4T OCA].	+	[[1c4t]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_bl21(de3) Escherichia coli bl21(de3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4T OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~10739245~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:010739245</ref><references group="xtra"/>
	[[Category: Dihydrolipoyllysine-residue succinyltransferase]]		[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
-	[[Category: Escherichia coli]]
	[[Category: Carroll, D.]]		[[Category: Carroll, D.]]
	[[Category: Ernst, S R.]]		[[Category: Ernst, S R.]]
Line 35:		Line 22:
	[[Category: Ketoglutarate dehydrogenase multienzyme complex]]		[[Category: Ketoglutarate dehydrogenase multienzyme complex]]
	[[Category: Transferase]]		[[Category: Transferase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 02:25:27 2009''