1gjx - Revision history

OCA at 05:30, 15 May 2024

OCA — Wed, 15 May 2024 05:30:11 GMT

←Older revision		Revision as of 05:30, 15 May 2024
Line 19:		Line 19:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gjx 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=1gjx ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The antigenic P64K protein from the pathogenic bacterium Neisseria meningitidis is found in the outer membrane of the cell, and consists of two parts: an 81-residue N-terminal region and a 482-residue C-terminal region. The amino-acid sequence of the N-terminal region is homologous with the lipoyl domains of the dihydrolipoyl acyltransferase (E2) components, and that of the C-terminal region with the dihydrolipoyl dehydrogenase (E3) components, of 2-oxo acid dehydrogenase multienzyme complexes. The two parts are separated by a long linker region, similar to the linker regions in the E2 chains of 2-oxo acid dehydrogenase complexes, and it is likely this region is conformationally flexible. A subgene encoding the P64K lipoyl domain was created and over-expressed in Escherichia coli. The product was capable of post-translational modification by the lipoate protein ligase but not aberrant modification by the biotin protein ligase of E. coli. The solution structure of the apo-domain was determined by means of heteronuclear NMR spectroscopy and found to be a flattened beta barrel composed of two four-stranded antiparallel beta sheets. The lysine residue that becomes lipoylated is in an exposed beta turn that, from a [1H]-15N heteronuclear Overhauser effect experiment, appears to enjoy substantial local motion. This structure of a lipoyl domain derived from a dihydrolipoyl dehydrogenase resembles that of lipoyl domains normally found as part of the dihydrolipoyl acyltransferase component of 2-oxo acid dehydrogenase complexes and will assist in furthering the understanding of its function in a multienzyme complex and in the membrane-bound P64K protein itself.
		+
		+	Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis.,Tozawa K, Broadhurst RW, Raine AR, Fuller C, Alvarez A, Guillen G, Padron G, Perham RN Eur J Biochem. 2001 Sep;268(18):4908-17. PMID:11559360<ref>PMID:11559360</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1gjx" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Pyruvate dehydrogenase 3D structures\|Pyruvate dehydrogenase 3D structures]]		*[[Pyruvate dehydrogenase 3D structures\|Pyruvate dehydrogenase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 11:21, 27 March 2024

OCA — Wed, 27 Mar 2024 11:21:53 GMT

←Older revision		Revision as of 11:21, 27 March 2024
Line 1:		Line 1:

	==Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis==		==Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis==
-	<StructureSection load='1gjx' size='340' side='right'caption='[[1gjx~~]], [[NMR_Ensembles_of_Models \| 18 NMR models~~]]' scene=''>	+	<StructureSection load='1gjx' size='340' side='right'caption='[[1gjx]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1gjx]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GJX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1gjx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GJX FirstGlance]. <br>
-	</td></tr><tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"~~><span class~~=~~'plainlinks'>[https://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </span~~></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjx OCA], [https://pdbe.org/1gjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gjx RCSB], [https://www.ebi.ac.uk/pdbsum/1gjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gjx 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=1gjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjx OCA], [https://pdbe.org/1gjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gjx RCSB], [https://www.ebi.ac.uk/pdbsum/1gjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gjx ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/Q9JZ09_NEIMB Q9JZ09_NEIMB]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 17:		Line 19:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gjx 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=1gjx ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The antigenic P64K protein from the pathogenic bacterium Neisseria meningitidis is found in the outer membrane of the cell, and consists of two parts: an 81-residue N-terminal region and a 482-residue C-terminal region. The amino-acid sequence of the N-terminal region is homologous with the lipoyl domains of the dihydrolipoyl acyltransferase (E2) components, and that of the C-terminal region with the dihydrolipoyl dehydrogenase (E3) components, of 2-oxo acid dehydrogenase multienzyme complexes. The two parts are separated by a long linker region, similar to the linker regions in the E2 chains of 2-oxo acid dehydrogenase complexes, and it is likely this region is conformationally flexible. A subgene encoding the P64K lipoyl domain was created and over-expressed in Escherichia coli. The product was capable of post-translational modification by the lipoate protein ligase but not aberrant modification by the biotin protein ligase of E. coli. The solution structure of the apo-domain was determined by means of heteronuclear NMR spectroscopy and found to be a flattened beta barrel composed of two four-stranded antiparallel beta sheets. The lysine residue that becomes lipoylated is in an exposed beta turn that, from a [1H]-15N heteronuclear Overhauser effect experiment, appears to enjoy substantial local motion. This structure of a lipoyl domain derived from a dihydrolipoyl dehydrogenase resembles that of lipoyl domains normally found as part of the dihydrolipoyl acyltransferase component of 2-oxo acid dehydrogenase complexes and will assist in furthering the understanding of its function in a multienzyme complex and in the membrane-bound P64K protein itself.
-
-	Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis.,Tozawa K, Broadhurst RW, Raine AR, Fuller C, Alvarez A, Guillen G, Padron G, Perham RN Eur J Biochem. 2001 Sep;268(18):4908-17. PMID:11559360<ref>PMID:11559360</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1gjx" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Pyruvate dehydrogenase 3D structures\|Pyruvate dehydrogenase 3D structures]]		*[[Pyruvate dehydrogenase 3D structures\|Pyruvate dehydrogenase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Dihydrolipoyl dehydrogenase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Alvarez, A]]	+	[[Category: Neisseria meningitidis]]
-	[[Category: Broadhurst~~, R W~~]]	+	[[Category: Alvarez A]]
-	[[Category: Fuller, C]]	+	[[Category: Broadhurst RW]]
-	[[Category: Guillen, G]]	+	[[Category: Fuller C]]
-	[[Category: Padron, G]]	+	[[Category: Guillen G]]
-	[[Category: Perham~~, R N~~]]	+	[[Category: Padron G]]
-	[[Category: Raine~~, A R.C~~]]	+	[[Category: Perham RN]]
-	[[Category: Tozawa, K]]	+	[[Category: Raine ARC]]
-	~~[[Category: Lipoyl domain]]~~	+	[[Category: Tozawa K]]
-	~~[[Category: Multienzyme complex]]~~	+
-	~~[[Category: Neisseria meningitidi]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Post-translational modification~~]]	+

OCA at 11:02, 31 March 2021

OCA — Wed, 31 Mar 2021 11:02:26 GMT

←Older revision		Revision as of 11:02, 31 March 2021
Line 3:		Line 3:
	<StructureSection load='1gjx' size='340' side='right'caption='[[1gjx]], [[NMR_Ensembles_of_Models \| 18 NMR models]]' scene=''>		<StructureSection load='1gjx' size='340' side='right'caption='[[1gjx]], [[NMR_Ensembles_of_Models \| 18 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1gjx]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1GJX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1gjx]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GJX FirstGlance]. <br>
-	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </span></td></tr>	+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </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=1gjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjx OCA], [~~http~~://pdbe.org/1gjx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1gjx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1gjx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1gjx 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=1gjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjx OCA], [https://pdbe.org/1gjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gjx RCSB], [https://www.ebi.ac.uk/pdbsum/1gjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gjx ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 28:		Line 28:

	==See Also==		==See Also==
-	*[[Pyruvate dehydrogenase\|Pyruvate dehydrogenase]]	+	*[[Pyruvate dehydrogenase 3D structures\|Pyruvate dehydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:54, 26 June 2019

OCA — Wed, 26 Jun 2019 07:54:59 GMT

←Older revision		Revision as of 07:54, 26 June 2019
Line 1:		Line 1:

	==Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis==		==Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis==
-	<StructureSection load='1gjx' size='340' side='right' caption='[[1gjx]], [[NMR_Ensembles_of_Models \| 18 NMR models]]' scene=''>	+	<StructureSection load='1gjx' size='340' side='right'caption='[[1gjx]], [[NMR_Ensembles_of_Models \| 18 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1gjx]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GJX FirstGlance]. <br>		<table><tr><td colspan='2'>[[1gjx]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GJX FirstGlance]. <br>
Line 11:		Line 11:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gj/1gjx_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gj/1gjx_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 34:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Dihydrolipoyl dehydrogenase]]		[[Category: Dihydrolipoyl dehydrogenase]]
		+	[[Category: Large Structures]]
	[[Category: Alvarez, A]]		[[Category: Alvarez, A]]
	[[Category: Broadhurst, R W]]		[[Category: Broadhurst, R W]]

OCA at 04:29, 21 September 2017

OCA — Thu, 21 Sep 2017 04:29:00 GMT

←Older revision		Revision as of 04:29, 21 September 2017
Line 1:		Line 1:
-	==~~SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE CHIMERIC DIHYDROLIPOYL DEHYDROGENASE~~ P64K ~~FROM NEISSERIA MENINGITIDIS~~==	+
		+	==Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis==
	<StructureSection load='1gjx' size='340' side='right' caption='[[1gjx]], [[NMR_Ensembles_of_Models \| 18 NMR models]]' scene=''>		<StructureSection load='1gjx' size='340' side='right' caption='[[1gjx]], [[NMR_Ensembles_of_Models \| 18 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1gjx]] is a 1 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/"diplokokkus_intracellularis_meningitidis"_(sic)_weichselbaum_1887 "diplokokkus intracellularis meningitidis" (sic) weichselbaum 1887]~~. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GJX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1gjx]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GJX FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </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=1gjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjx OCA], [http://pdbe.org/1gjx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gjx RCSB], [http://www.ebi.ac.uk/pdbsum/1gjx 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=1gjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjx OCA], [http://pdbe.org/1gjx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gjx RCSB], [http://www.ebi.ac.uk/pdbsum/1gjx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gjx ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 14:		Line 15:
	<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=1gjx ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 08:11, 11 September 2015

OCA — Fri, 11 Sep 2015 08:11:25 GMT

←Older revision		Revision as of 08:11, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1gjx' size='340' side='right' caption='[[1gjx]], [[NMR_Ensembles_of_Models \| 18 NMR models]]' scene=''>		<StructureSection load='1gjx' size='340' side='right' caption='[[1gjx]], [[NMR_Ensembles_of_Models \| 18 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1gjx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Neisseria_meningitidis Neisseria~~ meningitidis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GJX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1gjx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplokokkus_intracellularis_meningitidis"_(sic)_weichselbaum_1887 "diplokokkus intracellularis meningitidis" (sic) weichselbaum 1887]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GJX FirstGlance]. <br>
	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </span></td></tr>		</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </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=1gjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gjx RCSB], [http://www.ebi.ac.uk/pdbsum/1gjx 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=1gjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjx OCA], [http://pdbe.org/1gjx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gjx RCSB], [http://www.ebi.ac.uk/pdbsum/1gjx PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 24:		Line 24:
	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 1gjx" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Pyruvate dehydrogenase\|Pyruvate dehydrogenase]]
	== References ==		== References ==
	<references/>		<references/>
Line 29:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Dihydrolipoyl dehydrogenase]]		[[Category: Dihydrolipoyl dehydrogenase]]
-	[[Category: Neisseria meningitidis]]
	[[Category: Alvarez, A]]		[[Category: Alvarez, A]]
	[[Category: Broadhurst, R W]]		[[Category: Broadhurst, R W]]

OCA at 22:33, 22 December 2014

OCA — Mon, 22 Dec 2014 22:33:54 GMT

←Older revision		Revision as of 22:33, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1gjx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GJX FirstGlance]. <br>		<table><tr><td colspan='2'>[[1gjx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GJX FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </span></td></tr>	+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </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=1gjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gjx RCSB], [http://www.ebi.ac.uk/pdbsum/1gjx 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=1gjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gjx RCSB], [http://www.ebi.ac.uk/pdbsum/1gjx 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 30:		Line 30:
	[[Category: Dihydrolipoyl dehydrogenase]]		[[Category: Dihydrolipoyl dehydrogenase]]
	[[Category: Neisseria meningitidis]]		[[Category: Neisseria meningitidis]]
-	[[Category: Alvarez, A.]]	+	[[Category: Alvarez, A]]
-	[[Category: Broadhurst, R W.]]	+	[[Category: Broadhurst, R W]]
-	[[Category: Fuller, C.]]	+	[[Category: Fuller, C]]
-	[[Category: Guillen, G.]]	+	[[Category: Guillen, G]]
-	[[Category: Padron, G.]]	+	[[Category: Padron, G]]
-	[[Category: Perham, R N.]]	+	[[Category: Perham, R N]]
-	[[Category: Raine, A R.C.]]	+	[[Category: Raine, A R.C]]
-	[[Category: Tozawa, K~~.]]~~	+	[[Category: Tozawa, K]]
-	~~[[Category: Dihydrolipoyl dehydrogenase~~]]	+
	[[Category: Lipoyl domain]]		[[Category: Lipoyl domain]]
	[[Category: Multienzyme complex]]		[[Category: Multienzyme complex]]

OCA at 12:22, 28 September 2014

OCA — Sun, 28 Sep 2014 12:22:44 GMT

←Older revision		Revision as of 12:22, 28 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1gjx.~~png\|left~~\|200px]]	+	==SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE CHIMERIC DIHYDROLIPOYL DEHYDROGENASE P64K FROM NEISSERIA MENINGITIDIS==
		+	<StructureSection load='1gjx' size='340' side='right' caption='[[1gjx]], [[NMR_Ensembles_of_Models \| 18 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1gjx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GJX FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </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=1gjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gjx RCSB], [http://www.ebi.ac.uk/pdbsum/1gjx 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/gj/1gjx_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 antigenic P64K protein from the pathogenic bacterium Neisseria meningitidis is found in the outer membrane of the cell, and consists of two parts: an 81-residue N-terminal region and a 482-residue C-terminal region. The amino-acid sequence of the N-terminal region is homologous with the lipoyl domains of the dihydrolipoyl acyltransferase (E2) components, and that of the C-terminal region with the dihydrolipoyl dehydrogenase (E3) components, of 2-oxo acid dehydrogenase multienzyme complexes. The two parts are separated by a long linker region, similar to the linker regions in the E2 chains of 2-oxo acid dehydrogenase complexes, and it is likely this region is conformationally flexible. A subgene encoding the P64K lipoyl domain was created and over-expressed in Escherichia coli. The product was capable of post-translational modification by the lipoate protein ligase but not aberrant modification by the biotin protein ligase of E. coli. The solution structure of the apo-domain was determined by means of heteronuclear NMR spectroscopy and found to be a flattened beta barrel composed of two four-stranded antiparallel beta sheets. The lysine residue that becomes lipoylated is in an exposed beta turn that, from a [1H]-15N heteronuclear Overhauser effect experiment, appears to enjoy substantial local motion. This structure of a lipoyl domain derived from a dihydrolipoyl dehydrogenase resembles that of lipoyl domains normally found as part of the dihydrolipoyl acyltransferase component of 2-oxo acid dehydrogenase complexes and will assist in furthering the understanding of its function in a multienzyme complex and in the membrane-bound P64K protein itself.

-	~~{{STRUCTURE_1gjx\| PDB=1gjx \| SCENE= }}~~	+	Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis.,Tozawa K, Broadhurst RW, Raine AR, Fuller C, Alvarez A, Guillen G, Padron G, Perham RN Eur J Biochem. 2001 Sep;268(18):4908-17. PMID:11559360<ref>PMID:11559360</ref>

-	~~===SOLUTION STRUCTURE OF THE LIPOYL DOMAIN OF THE CHIMERIC DIHYDROLIPOYL DEHYDROGENASE P64K FROM NEISSERIA MENINGITIDIS===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_11559360}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1gjx]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Neisseria_meningitidis Neisseria meningitidis]~~. ~~Full experimental information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA].~~	+	</StructureSection>
-		+
-	==~~See Also==~~	+
-	*[[Pyruvate dehydrogenase\|Pyruvate dehydrogenase]]	+
-		+
-	~~==Reference~~==	+
-	<~~ref group="xtra">PMID:011559360<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Dihydrolipoyl dehydrogenase]]		[[Category: Dihydrolipoyl dehydrogenase]]
	[[Category: Neisseria meningitidis]]		[[Category: Neisseria meningitidis]]

OCA at 17:21, 20 October 2012

OCA — Sat, 20 Oct 2012 17:21:58 GMT

←Older revision		Revision as of 17:21, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1gjx]] is a 1 chain structure ~~of [[Pyruvate dehydrogenase]]~~ with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA].	+	[[1gjx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJX OCA].

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

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

OCA — Fri, 27 Jul 2012 00:40:53 GMT

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

←Older revision

Revision as of 00:40, 27 July 2012