2cyu - Revision history

OCA at 11:32, 22 May 2024

OCA — Wed, 22 May 2024 11:32:34 GMT

←Older revision		Revision as of 11:32, 22 May 2024
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	==NMR structure of a downhill folding protein==		==NMR structure of a downhill folding protein==
-	<StructureSection load='2cyu' size='340' side='right'caption='[[2cyu~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='2cyu' size='340' side='right'caption='[[2cyu]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2cyu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CYU FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2cyu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CYU FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=NAL:BETA-(2-NAPHTHYL)-ALANINE'>NAL</scene~~></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='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1bbl\|1bbl]], [[1bal\|1bal]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAL:BETA-(2-NAPHTHYL)-ALANINE'>NAL</scene></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=2cyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyu OCA], [https://pdbe.org/2cyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cyu RCSB], [https://www.ebi.ac.uk/pdbsum/2cyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cyu 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=2cyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyu OCA], [https://pdbe.org/2cyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cyu RCSB], [https://www.ebi.ac.uk/pdbsum/2cyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cyu ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ODO2_ECO57 ODO2_ECO57]] 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) (By similarity).	+	[https://www.uniprot.org/uniprot/ODO2_ECO57 ODO2_ECO57] 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) (By similarity).
	== 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: Escherichia coli O157:H7]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Munoz, V]]	+	[[Category: Munoz V]]
-	[[Category: Sadqi, M]]	+	[[Category: Sadqi M]]
-	~~[[Category: Downhill folding protein]]~~	+
-	~~[[Category: Helix bundle]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 10:24, 8 December 2021

OCA — Wed, 08 Dec 2021 10:24:01 GMT

←Older revision		Revision as of 10:24, 8 December 2021
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	<StructureSection load='2cyu' size='340' side='right'caption='[[2cyu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2cyu' size='340' side='right'caption='[[2cyu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2cyu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYU OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2CYU FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2cyu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CYU FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAL:BETA-(2-NAPHTHYL)-ALANINE'>NAL</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAL:BETA-(2-NAPHTHYL)-ALANINE'>NAL</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bbl\|1bbl]], [[1bal\|1bal]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bbl\|1bbl]], [[1bal\|1bal]]</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=2cyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyu OCA], [~~http~~://pdbe.org/2cyu PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2cyu RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2cyu PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2cyu 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=2cyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyu OCA], [https://pdbe.org/2cyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cyu RCSB], [https://www.ebi.ac.uk/pdbsum/2cyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cyu ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ODO2_ECO57 ODO2_ECO57]] 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) (By similarity).	+	[[https://www.uniprot.org/uniprot/ODO2_ECO57 ODO2_ECO57]] 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) (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:34, 4 March 2020

OCA — Wed, 04 Mar 2020 07:34:46 GMT

←Older revision		Revision as of 07:34, 4 March 2020
Line 1:		Line 1:

	==NMR structure of a downhill folding protein==		==NMR structure of a downhill folding protein==
-	<StructureSection load='2cyu' size='340' side='right' caption='[[2cyu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='2cyu' size='340' side='right'caption='[[2cyu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2cyu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CYU FirstGlance]. <br>		<table><tr><td colspan='2'>[[2cyu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CYU FirstGlance]. <br>
Line 32:		Line 32:

	==See Also==		==See Also==
-	*[[2-~~Oxoglutarate Dehydrogenase~~\|2-~~Oxoglutarate Dehydrogenase~~]]	+	*[[2-oxoglutarate dehydrogenase 3D structures\|2-oxoglutarate dehydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Dihydrolipoyllysine-residue succinyltransferase]]		[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
		+	[[Category: Large Structures]]
	[[Category: Munoz, V]]		[[Category: Munoz, V]]
	[[Category: Sadqi, M]]		[[Category: Sadqi, M]]

OCA at 06:13, 30 May 2018

OCA — Wed, 30 May 2018 06:13:36 GMT

←Older revision		Revision as of 06:13, 30 May 2018
Line 1:		Line 1:
		+
	==NMR structure of a downhill folding protein==		==NMR structure of a downhill folding protein==
	<StructureSection load='2cyu' size='340' side='right' caption='[[2cyu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2cyu' size='340' side='right' caption='[[2cyu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bbl\|1bbl]], [[1bal\|1bal]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bbl\|1bbl]], [[1bal\|1bal]]</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=2cyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyu OCA], [http://pdbe.org/2cyu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cyu RCSB], [http://www.ebi.ac.uk/pdbsum/2cyu 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=2cyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyu OCA], [http://pdbe.org/2cyu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cyu RCSB], [http://www.ebi.ac.uk/pdbsum/2cyu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cyu ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cy/2cyu_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cy/2cyu_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 07:29, 10 February 2016

OCA — Wed, 10 Feb 2016 07:29:32 GMT

←Older revision		Revision as of 07:29, 10 February 2016
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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=2cyu ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 06:42, 11 September 2015

OCA — Fri, 11 Sep 2015 06:42:12 GMT

←Older revision		Revision as of 06:42, 11 September 2015
Line 6:		Line 6:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bbl\|1bbl]], [[1bal\|1bal]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bbl\|1bbl]], [[1bal\|1bal]]</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=2cyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cyu RCSB], [http://www.ebi.ac.uk/pdbsum/2cyu 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=2cyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyu OCA], [http://pdbe.org/2cyu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cyu RCSB], [http://www.ebi.ac.uk/pdbsum/2cyu 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 2cyu" style="background-color:#fffaf0;"></div>

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

OCA at 12:44, 25 December 2014

OCA — Thu, 25 Dec 2014 12:44:04 GMT

←Older revision		Revision as of 12:44, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2cyu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CYU FirstGlance]. <br>		<table><tr><td colspan='2'>[[2cyu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CYU FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAL:BETA-(2-NAPHTHYL)-ALANINE'>NAL</scene></td></tr>	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAL:BETA-(2-NAPHTHYL)-ALANINE'>NAL</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bbl\|1bbl]], [[1bal\|1bal]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bbl\|1bbl]], [[1bal\|1bal]]</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=2cyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cyu RCSB], [http://www.ebi.ac.uk/pdbsum/2cyu 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=2cyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cyu RCSB], [http://www.ebi.ac.uk/pdbsum/2cyu PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ODO2_ECO57 ODO2_ECO57]] 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) (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Dihydrolipoyllysine-residue succinyltransferase]]		[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
-	[[Category: Munoz, V.]]	+	[[Category: Munoz, V]]
-	[[Category: Sadqi, M.]]	+	[[Category: Sadqi, M]]
	[[Category: Downhill folding protein]]		[[Category: Downhill folding protein]]
	[[Category: Helix bundle]]		[[Category: Helix bundle]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 03:53, 29 September 2014

OCA — Mon, 29 Sep 2014 03:53:43 GMT

←Older revision		Revision as of 03:53, 29 September 2014
Line 1:		Line 1:
-	[[~~Image:~~2cyu.~~png~~\|~~left~~\|200px]]	+	==NMR structure of a downhill folding protein==
		+	<StructureSection load='2cyu' size='340' side='right' caption='[[2cyu]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2cyu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CYU FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAL:BETA-(2-NAPHTHYL)-ALANINE'>NAL</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bbl\|1bbl]], [[1bal\|1bal]]</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=2cyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cyu RCSB], [http://www.ebi.ac.uk/pdbsum/2cyu 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/cy/2cyu_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 ==
		+	Protein folding is an inherently complex process involving coordination of the intricate networks of weak interactions that stabilize native three-dimensional structures. In the conventional paradigm, simple protein structures are assumed to fold in an all-or-none process that is inaccessible to experiment. Existing experimental methods therefore probe folding mechanisms indirectly. A widely used approach interprets changes in protein stability and/or folding kinetics, induced by engineered mutations, in terms of the structure of the native protein. In addition to limitations in connecting energetics with structure, mutational methods have significant experimental uncertainties and are unable to map complex networks of interactions. In contrast, analytical theory predicts small barriers to folding and the possibility of downhill folding. These theoretical predictions have been confirmed experimentally in recent years, including the observation of global downhill folding. However, a key remaining question is whether downhill folding can indeed lead to the high-resolution analysis of protein folding processes. Here we show, with the use of nuclear magnetic resonance (NMR), that the downhill protein BBL from Escherichia coli unfolds atom by atom starting from a defined three-dimensional structure. Thermal unfolding data on 158 backbone and side-chain protons out of a total of 204 provide a detailed view of the structural events during folding. This view confirms the statistical nature of folding, and exposes the interplay between hydrogen bonding, hydrophobic forces, backbone conformation and side-chain entropy. From the data we also obtain a map of the interaction network in this protein, which reveals the source of folding cooperativity. Our approach can be extended to other proteins with marginal barriers (less than 3RT), providing a new tool for the study of protein folding.

-	~~{{STRUCTURE_2cyu\| PDB=2cyu \| SCENE= }}~~	+	Atom-by-atom analysis of global downhill protein folding.,Sadqi M, Fushman D, Munoz V Nature. 2006 Jul 20;442(7100):317-21. Epub 2006 Jun 14. PMID:16799571<ref>PMID:16799571</ref>

-	~~===NMR structure~~ of ~~a downhill folding protein===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_16799571}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2cyu]] is a 1 chain structure~~. ~~Full experimental information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=2CYU OCA].~~	+

	==See Also==		==See Also==
	*[[2-Oxoglutarate Dehydrogenase\|2-Oxoglutarate Dehydrogenase]]		*[[2-Oxoglutarate Dehydrogenase\|2-Oxoglutarate Dehydrogenase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:016799571<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Dihydrolipoyllysine-residue succinyltransferase]]		[[Category: Dihydrolipoyllysine-residue succinyltransferase]]
	[[Category: Munoz, V.]]		[[Category: Munoz, V.]]

OCA at 16:48, 20 October 2012

OCA — Sat, 20 Oct 2012 16:48:58 GMT

←Older revision		Revision as of 16:48, 20 October 2012
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	==About this Structure==		==About this Structure==
-	[[2cyu]] is a 1 chain structure ~~of [[2-Oxoglutarate Dehydrogenase]]~~. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYU OCA].	+	[[2cyu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYU OCA].

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

OCA: Protected "2cyu" [edit=sysop:move=sysop]

OCA — Thu, 26 Jul 2012 22:54:35 GMT

Protected "2cyu" [edit=sysop:move=sysop]

←Older revision

Revision as of 22:54, 26 July 2012