6scg - Revision history

OCA at 12:39, 24 January 2024

OCA — Wed, 24 Jan 2024 12:39:27 GMT

←Older revision		Revision as of 12:39, 24 January 2024
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	<StructureSection load='6scg' size='340' side='right'caption='[[6scg]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='6scg' size='340' side='right'caption='[[6scg]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6scg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Escherichia_coli_m114~~ Escherichia coli ~~m114~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SCG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6scg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SCG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <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]] 1.65Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6sci\|6sci]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">adhE, ana, b1241, JW1228 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=656416 Escherichia coli M114])</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=6scg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6scg OCA], [https://pdbe.org/6scg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6scg RCSB], [https://www.ebi.ac.uk/pdbsum/6scg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6scg 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=6scg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6scg OCA], [https://pdbe.org/6scg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6scg RCSB], [https://www.ebi.ac.uk/pdbsum/6scg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6scg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ADHE_ECOLI ADHE_ECOLI]] This enzyme has three activities: ADH, ACDH, and PFL-deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction.	+	[https://www.uniprot.org/uniprot/ADHE_ECOLI ADHE_ECOLI] This enzyme has three activities: ADH, ACDH, and PFL-deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Escherichia coli ~~m114~~]]	+	[[Category: Escherichia coli K-12]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bragginton, E]]	+	[[Category: Bragginton E]]
-	[[Category: Lovering~~, A L]]~~	+	[[Category: Lovering AL]]
-	~~[[Category: Aldehyde alcohol dehydrogenase]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 06:52, 17 March 2021

OCA — Wed, 17 Mar 2021 06:52:09 GMT

←Older revision		Revision as of 06:52, 17 March 2021
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	==Structure of AdhE form 1==		==Structure of AdhE form 1==
-	<StructureSection load='6scg' size='340' side='right'caption='[[6scg]]' scene=''>	+	<StructureSection load='6scg' size='340' side='right'caption='[[6scg]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SCG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6SCG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6scg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_m114 Escherichia coli m114]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SCG FirstGlance]. <br>
-	</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=6scg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6scg OCA], [~~http~~://pdbe.org/6scg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6scg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6scg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6scg ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6sci\|6sci]]</div></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">adhE, ana, b1241, JW1228 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=656416 Escherichia coli M114])</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=6scg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6scg OCA], [https://pdbe.org/6scg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6scg RCSB], [https://www.ebi.ac.uk/pdbsum/6scg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6scg ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/ADHE_ECOLI ADHE_ECOLI]] This enzyme has three activities: ADH, ACDH, and PFL-deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The bifunctional alcohol/aldehyde dehydrogenase (AdhE) comprises both an N-terminal aldehyde dehydrogenase (AldDH) and a C-terminal alcohol dehydrogenase (ADH). In vivo, full-length AdhE oligomerizes into long oligomers known as spirosomes. However, structural analysis of AdhE is challenging owing to the heterogeneity of the spirosomes. Therefore, the domains of AdhE are best characterized separately. Here, the structure of ADH from the pathogenic Escherichia coli O157:H7 was determined to 1.65 A resolution. The dimeric crystal structure was confirmed in solution by small-angle X-ray scattering.
		+
		+	High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE.,Azmi L, Bragginton EC, Cadby IT, Byron O, Roe AJ, Lovering AL, Gabrielsen M Acta Crystallogr F Struct Biol Commun. 2020 Sep 1;76(Pt 9):414-421. doi:, 10.1107/S2053230X20010237. Epub 2020 Aug 19. PMID:32880589<ref>PMID:32880589</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6scg" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Escherichia coli m114]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bragginton E]]	+	[[Category: Bragginton, E]]
-	[[Category: Lovering AL]]	+	[[Category: Lovering, A L]]
		+	[[Category: Aldehyde alcohol dehydrogenase]]
		+	[[Category: Oxidoreductase]]

OCA at 11:13, 26 August 2020

OCA — Wed, 26 Aug 2020 11:13:00 GMT

←Older revision		Revision as of 11:13, 26 August 2020
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-	'''Unreleased structure'''

-	~~The entry~~ 6scg ~~is ON HOLD until Paper Publication~~	+	==Structure of AdhE form 1==
-		+	<StructureSection load='6scg' size='340' side='right'caption='[[6scg]]' scene=''>
-	~~Authors~~: ~~Lovering~~, A.L., ~~Bragginton~~, E.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SCG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SCG FirstGlance]. <br>
-	~~Description: Structure of AdhE form 1~~	+	</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=6scg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6scg OCA], [http://pdbe.org/6scg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6scg RCSB], [http://www.ebi.ac.uk/pdbsum/6scg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6scg ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: Bragginton, E]]	+	__TOC__
-	[[Category: Lovering~~, A.L~~]]	+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Bragginton E]]
		+	[[Category: Lovering AL]]

OCA at 09:18, 29 July 2020

OCA — Wed, 29 Jul 2020 09:18:03 GMT

←Older revision		Revision as of 09:18, 29 July 2020
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6scg is ON HOLD	+	The entry 6scg is ON HOLD until Paper Publication

	Authors: Lovering, A.L., Bragginton, E.		Authors: Lovering, A.L., Bragginton, E.

OCA: Protected "6scg" [edit=sysop:move=sysop]

OCA — Wed, 31 Jul 2019 04:57:42 GMT

Protected "6scg" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:57, 31 July 2019

OCA: New page: '''Unreleased structure''' The entry 6scg is ON HOLD Authors: Lovering, A.L., Bragginton, E. Description: Structure of AdhE form 1 Category: Unreleased Structures [[Category: Bragg...

OCA — Wed, 31 Jul 2019 04:57:40 GMT

New page: '''Unreleased structure''' The entry 6scg is ON HOLD Authors: Lovering, A.L., Bragginton, E. Description: Structure of AdhE form 1 Category: Unreleased Structures [[Category: Bragg...

New page

'''Unreleased structure'''

The entry 6scg is ON HOLD

Authors: Lovering, A.L., Bragginton, E.

Description: Structure of AdhE form 1
[[Category: Unreleased Structures]]
[[Category: Bragginton, E]]
[[Category: Lovering, A.L]]