3lad - Revision history

OCA at 07:05, 7 October 2020

OCA — Wed, 07 Oct 2020 07:05:37 GMT

←Older revision		Revision as of 07:05, 7 October 2020
Line 1:		Line 1:

	==REFINED CRYSTAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM AZOTOBACTER VINELANDII AT 2.2 ANGSTROMS RESOLUTION. A COMPARISON WITH THE STRUCTURE OF GLUTATHIONE REDUCTASE==		==REFINED CRYSTAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM AZOTOBACTER VINELANDII AT 2.2 ANGSTROMS RESOLUTION. A COMPARISON WITH THE STRUCTURE OF GLUTATHIONE REDUCTASE==
-	<StructureSection load='3lad' size='340' side='right' caption='[[3lad]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='3lad' size='340' side='right'caption='[[3lad]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3lad]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAD OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3LAD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3lad]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3LAD FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></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='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=3lad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lad OCA], [http://pdbe.org/3lad PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lad RCSB], [http://www.ebi.ac.uk/pdbsum/3lad PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lad ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3lad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lad OCA], [http://pdbe.org/3lad PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lad RCSB], [http://www.ebi.ac.uk/pdbsum/3lad PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lad ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 38:		Line 38:
	[[Category: Atcc 478]]		[[Category: Atcc 478]]
	[[Category: Dihydrolipoyl dehydrogenase]]		[[Category: Dihydrolipoyl dehydrogenase]]
		+	[[Category: Large Structures]]
	[[Category: Hol, W G.J]]		[[Category: Hol, W G.J]]
	[[Category: Mattevi, A]]		[[Category: Mattevi, A]]
	[[Category: Schierbeek, A J]]		[[Category: Schierbeek, A J]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 06:52, 2 January 2019

OCA — Wed, 02 Jan 2019 06:52:57 GMT

←Older revision		Revision as of 06:52, 2 January 2019
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/la/3lad_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/la/3lad_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 12:14, 5 August 2016

OCA — Fri, 05 Aug 2016 12:14:55 GMT

←Older revision		Revision as of 12:14, 5 August 2016
Line 1:		Line 1:
		+
	==REFINED CRYSTAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM AZOTOBACTER VINELANDII AT 2.2 ANGSTROMS RESOLUTION. A COMPARISON WITH THE STRUCTURE OF GLUTATHIONE REDUCTASE==		==REFINED CRYSTAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM AZOTOBACTER VINELANDII AT 2.2 ANGSTROMS RESOLUTION. A COMPARISON WITH THE STRUCTURE OF GLUTATHIONE REDUCTASE==
	<StructureSection load='3lad' size='340' side='right' caption='[[3lad]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='3lad' size='340' side='right' caption='[[3lad]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3lad]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Azotobacter_vinelandii Azotobacter vinelandii~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LAD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3lad]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_478 Atcc 478]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LAD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></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='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=3lad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lad OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lad RCSB], [http://www.ebi.ac.uk/pdbsum/3lad 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=3lad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lad OCA], [http://pdbe.org/3lad PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lad RCSB], [http://www.ebi.ac.uk/pdbsum/3lad PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lad ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lad ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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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 3lad" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Azotobacter vinelandii~~]]	+	[[Category: Atcc 478]]
	[[Category: Dihydrolipoyl dehydrogenase]]		[[Category: Dihydrolipoyl dehydrogenase]]
	[[Category: Hol, W G.J]]		[[Category: Hol, W G.J]]

OCA at 18:45, 25 December 2014

OCA — Thu, 25 Dec 2014 18:45:28 GMT

←Older revision		Revision as of 18:45, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3lad]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LAD FirstGlance]. <br>		<table><tr><td colspan='2'>[[3lad]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LAD FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></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 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=3lad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lad OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lad RCSB], [http://www.ebi.ac.uk/pdbsum/3lad 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=3lad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lad OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lad RCSB], [http://www.ebi.ac.uk/pdbsum/3lad PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DLDH_AZOVI DLDH_AZOVI]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 36:
	[[Category: Azotobacter vinelandii]]		[[Category: Azotobacter vinelandii]]
	[[Category: Dihydrolipoyl dehydrogenase]]		[[Category: Dihydrolipoyl dehydrogenase]]
-	[[Category: Hol, W G.J.]]	+	[[Category: Hol, W G.J]]
-	[[Category: Mattevi, A.]]	+	[[Category: Mattevi, A]]
-	[[Category: Schierbeek, A J.]]	+	[[Category: Schierbeek, A J]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 13:06, 29 September 2014

OCA — Mon, 29 Sep 2014 13:06:54 GMT

←Older revision		Revision as of 13:06, 29 September 2014
Line 1:		Line 1:
-	[[~~Image~~:3lad.~~png\|left~~\|200px]]	+	==REFINED CRYSTAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM AZOTOBACTER VINELANDII AT 2.2 ANGSTROMS RESOLUTION. A COMPARISON WITH THE STRUCTURE OF GLUTATHIONE REDUCTASE==
		+	<StructureSection load='3lad' size='340' side='right' caption='[[3lad]], [[Resolution\|resolution]] 2.20Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3lad]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LAD FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene><br>
		+	<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=3lad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lad OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lad RCSB], [http://www.ebi.ac.uk/pdbsum/3lad PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/la/3lad_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The structure of lipoamide dehydrogenase from Azotobacter vinelandii has been refined by the molecular dynamics technique to an R-factor of 19.8% at 2.2 A resolution. In the final model, the root-mean-square deviation from ideality is 0.02 A for bond lengths and 3.2 degrees for bond angles. The asymmetric unit comprises two subunits, each consisting of 466 amino acid residues and the prosthetic group FAD, plus 512 solvent molecules. The last ten amino acid residues of both chains are not visible in the electron density distribution and they are probably disordered. The operation required to superimpose the two chains forming the dimer is a rotation of exactly 180 degrees with no translation component. The final model shows the two independently refined subunits to be very similar, except for six loops located at the surface of the molecule. The structure of each subunit of the enzyme consists of four domains with the catalytic centre located at the subunit interface. The reactive disulphide bridge, 48-53, is oxidized with S gamma of Cys53 located 3.5 A away from carbon C-4a of the isoalloxazine ring. The side-chain of His450' points its N epsilon 2 towards S gamma of Cys48 and is hydrogen bonded to the carboxylate of Glu455'. The FAD is bound in an extended conformation and the isoalloxazine ring is not completely planar with an angle between the pteridine and the benzene ring of 7.3 degrees in the first subunit and of 12.1 degrees in the second one. The overall folding of lipoamide dehydrogenase is very similar to that of glutathione reductase. However, a comparison of the two enzymes, which have only 26% sequence identity, reveals significant conformational differences. These concern the tertiary as well as the quaternary structure of the two molecules. In each subunit of lipoamide dehydrogenase the NAD-binding domain and the interface domain appear to be differently oriented with respect to the FAD-binding domain by 7.1 degrees and 7.8 degrees, respectively. The interface domain contains, in addition, major changes in tertiary structure. Furthermore, the two subunits forming the dimer appear to be shifted with respect to each other by more than 4 A, when the lipoamide dehydrogenase dimer is compared with that of glutathione reductase. In spite of all these changes at the tertiary and quaternary level the active sites of the enzymes, which occur at the dimer interface, appear to be remarkably similar.(ABSTRACT TRUNCATED AT 400 WORDS)

-	~~{{STRUCTURE_3lad\| PDB=3lad \| SCENE= }}~~	+	Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 A resolution. A comparison with the structure of glutathione reductase.,Mattevi A, Schierbeek AJ, Hol WG J Mol Biol. 1991 Aug 20;220(4):975-94. PMID:1880807<ref>PMID:1880807</ref>

-	~~===REFINED CRYSTAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM AZOTOBACTER VINELANDII AT 2.2 ANGSTROMS RESOLUTION. A COMPARISON WITH THE STRUCTURE OF GLUTATHIONE REDUCTASE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_1880807}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3lad]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3LAD OCA].~~	+

	==See Also==		==See Also==
	*[[Dihydrolipoamide dehydrogenase\|Dihydrolipoamide dehydrogenase]]		*[[Dihydrolipoamide dehydrogenase\|Dihydrolipoamide dehydrogenase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:001880807<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Azotobacter vinelandii]]		[[Category: Azotobacter vinelandii]]
	[[Category: Dihydrolipoyl dehydrogenase]]		[[Category: Dihydrolipoyl dehydrogenase]]

OCA at 20:08, 20 October 2012

OCA — Sat, 20 Oct 2012 20:08:48 GMT

←Older revision		Revision as of 20:08, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3lad]] is a 2 chain structure ~~of [[Dihydrolipoamide dehydrogenase]]~~ with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAD OCA].	+	[[3lad]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAD OCA].

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

OCA: Protected "3lad" [edit=sysop:move=sysop]

OCA — Fri, 27 Jul 2012 09:33:20 GMT

Protected "3lad" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:33, 27 July 2012

OCA at 09:33, 27 July 2012

OCA — Fri, 27 Jul 2012 09:33:17 GMT

←Older revision		Revision as of 09:33, 27 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:3lad.png\|left\|200px]]		[[Image:3lad.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3lad", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3lad\| PDB=3lad \| SCENE= }}		{{STRUCTURE_3lad\| PDB=3lad \| SCENE= }}

	===REFINED CRYSTAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM AZOTOBACTER VINELANDII AT 2.2 ANGSTROMS RESOLUTION. A COMPARISON WITH THE STRUCTURE OF GLUTATHIONE REDUCTASE===		===REFINED CRYSTAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM AZOTOBACTER VINELANDII AT 2.2 ANGSTROMS RESOLUTION. A COMPARISON WITH THE STRUCTURE OF GLUTATHIONE REDUCTASE===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_1880807}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 1880807 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_1880807}}		{{ABSTRACT_PUBMED_1880807}}

	==About this Structure==		==About this Structure==
-	~~3LAD~~ is a 2 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAD OCA].	+	[[3lad]] is a 2 chain structure of [[Dihydrolipoamide dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAD OCA].
		+
		+	==See Also==
		+	*[[Dihydrolipoamide dehydrogenase\|Dihydrolipoamide dehydrogenase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~1880807~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:001880807</ref><references group="xtra"/>
	[[Category: Azotobacter vinelandii]]		[[Category: Azotobacter vinelandii]]
	[[Category: Dihydrolipoyl dehydrogenase]]		[[Category: Dihydrolipoyl dehydrogenase]]
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	[[Category: Schierbeek, A J.]]		[[Category: Schierbeek, A J.]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 02:54:26 2009''

OCA at 00:54, 18 February 2009

OCA — Wed, 18 Feb 2009 00:54:28 GMT

←Older revision		Revision as of 00:54, 18 February 2009
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	==About this Structure==		==About this Structure==
-	3LAD is a ~~[[Single protein]]~~ structure of ~~sequence~~ from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAD OCA].	+	3LAD is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LAD OCA].

	==Reference==		==Reference==
-	Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 A resolution. A comparison with the structure of glutathione reductase., Mattevi A, Schierbeek AJ, Hol WG, J Mol Biol. 1991 Aug 20;220(4):975-94. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/1880807 1880807]~~	+	<ref group="xtra">PMID:1880807</ref><references group="xtra"/>
	[[Category: Azotobacter vinelandii]]		[[Category: Azotobacter vinelandii]]
	[[Category: Dihydrolipoyl dehydrogenase]]		[[Category: Dihydrolipoyl dehydrogenase]]
-	[[Category: Single protein]]
	[[Category: Hol, W G.J.]]		[[Category: Hol, W G.J.]]
	[[Category: Mattevi, A.]]		[[Category: Mattevi, A.]]
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	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

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OCA — Thu, 03 Jul 2008 09:52:30 GMT

←Older revision		Revision as of 09:52, 3 July 2008
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-	[[Image:3lad.~~jpg~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:3lad.png\|left\|200px]]

	<!--		<!--
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	{{STRUCTURE_3lad\| PDB=3lad \| SCENE= }}		{{STRUCTURE_3lad\| PDB=3lad \| SCENE= }}

-	~~'''~~REFINED CRYSTAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM AZOTOBACTER VINELANDII AT 2.2 ANGSTROMS RESOLUTION. A COMPARISON WITH THE STRUCTURE OF GLUTATHIONE REDUCTASE~~'''~~	+	===REFINED CRYSTAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM AZOTOBACTER VINELANDII AT 2.2 ANGSTROMS RESOLUTION. A COMPARISON WITH THE STRUCTURE OF GLUTATHIONE REDUCTASE===


-	~~==Overview==~~	+	<!--
-	~~The structure of lipoamide dehydrogenase from Azotobacter vinelandii has been refined by the molecular dynamics technique to an R~~-~~factor of 19.8% at 2.2 A resolution. In the final model, the root~~-~~mean-square deviation from ideality is 0.02 A for bond lengths and 3.2 degrees for bond angles.~~ The ~~asymmetric unit comprises two subunits~~, ~~each consisting of 466 amino acid residues and the prosthetic group FAD~~, ~~plus 512 solvent molecules. The last ten amino acid residues of both chains are not visible in~~ the ~~electron density distribution and they are probably disordered. The operation required~~ to ~~superimpose~~ the two chains forming the dimer is a rotation of exactly 180 degrees with no translation component. The final model shows the two independently refined subunits to be very similar, except for six loops located at ~~the surface of the molecule~~. ~~The structure of each subunit of the enzyme consists of four domains with the catalytic centre located at the subunit interface~~. ~~The reactive disulphide bridge, 48-53~~, is ~~oxidized with S gamma of Cys53 located 3.5 A away from carbon C-4a of~~ the ~~isoalloxazine ring~~. ~~The side~~-chain of His450' points its N epsilon 2 towards S gamma of Cys48 and is hydrogen bonded to the carboxylate of Glu455'. The FAD is bound in an extended conformation and the isoalloxazine ring is not completely planar with an angle between the pteridine and the benzene ring of 7.3 degrees in the first subunit and of 12.1 degrees in the second one. The overall folding of lipoamide dehydrogenase is very similar to that of glutathione reductase. However, a comparison of the two enzymes, which have only 26% sequence identity, reveals significant conformational differences. These concern the tertiary as well as the quaternary structure of the two molecules. In each subunit of lipoamide dehydrogenase the NAD-binding domain and the interface domain appear to be differently oriented with respect to the FAD-binding domain by 7.1 degrees and 7.8 degrees, respectively. The interface domain contains, in addition, major changes in tertiary structure. Furthermore, the two subunits forming the dimer appear to be shifted with respect to each other by more than 4 A, when the lipoamide dehydrogenase dimer is compared with that of glutathione reductase. In spite of all these changes at the tertiary and quaternary level the active sites of the enzymes, which occur at the dimer interface, appear to be remarkably similar.(ABSTRACT TRUNCATED AT 400 WORDS)	+	The line below this paragraph, {{ABSTRACT_PUBMED_1880807}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 1880807 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_1880807}}

	==About this Structure==		==About this Structure==
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	[[Category: Schierbeek, A J.]]		[[Category: Schierbeek, A J.]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May~~ ~~4 22~~:05:24 2008''	+
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