3fpc - Revision history

OCA at 15:31, 1 November 2023

2023-11-01T15:31:01Z

← Older revision		Revision as of 15:31, 1 November 2023
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	<StructureSection load='3fpc' size='340' side='right'caption='[[3fpc]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='3fpc' size='340' side='right'caption='[[3fpc]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3fpc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Enthi Enthi~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FPC FirstGlance]. <br>		<table><tr><td colspan='2'>[[3fpc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica] and [https://en.wikipedia.org/wiki/Thermoanaerobacter_brockii Thermoanaerobacter brockii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FPC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.4Å</td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3fpl\|3fpl]]</div></td></tr>~~		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ADH1, ADH1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5759 ENTHI])</td></tr>~~
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] </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=3fpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fpc OCA], [https://pdbe.org/3fpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fpc RCSB], [https://www.ebi.ac.uk/pdbsum/3fpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fpc 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=3fpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fpc OCA], [https://pdbe.org/3fpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fpc RCSB], [https://www.ebi.ac.uk/pdbsum/3fpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fpc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/ADH_THEBR ADH_THEBR]] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.		[https://www.uniprot.org/uniprot/ADH_THEBR ADH_THEBR] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.[https://www.uniprot.org/uniprot/ADH1_ENTHI ADH1_ENTHI] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.<ref>PMID:20102159</ref>
	== 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: ~~Enthi~~]]		[[Category: Entamoeba histolytica]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Burstein, Y]]		[[Category: Thermoanaerobacter brockii]]
	[[Category: Felix, F]]		[[Category: Burstein Y]]
	[[Category: Goihberg, E]]		[[Category: Felix F]]
	[[Category: Shimon, L]]		[[Category: Goihberg E]]
	~~[[Category: Bacterial alcohol dehydrogenase]]~~		[[Category: Shimon L]]
	~~[[Category: Chimera]]~~
	~~[[Category: Domain exchange]]~~
	~~[[Category: Metal-binding]]~~
	~~[[Category: Nadp]]~~
	~~[[Category: Oxidoreductase]]~~
	~~[[Category: Oxydoreductase~~]]

OCA at 08:07, 2 March 2022

2022-03-02T08:07:20Z

← Older revision		Revision as of 08:07, 2 March 2022
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	==Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH==		==Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH==
	<StructureSection load='3fpc' size='340' side='right' caption='[[3fpc]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='3fpc' size='340' side='right'caption='[[3fpc]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3fpc]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Enthi Enthi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FPC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3FPC FirstGlance]. <br>		<table><tr><td colspan='2'>[[3fpc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Enthi Enthi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FPC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3fpl\|3fpl]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3fpl\|3fpl]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ADH1, ADH1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5759 ENTHI])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ADH1, ADH1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5759 ENTHI])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] </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=3fpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fpc OCA], [~~http~~://pdbe.org/3fpc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3fpc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3fpc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3fpc 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=3fpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fpc OCA], [https://pdbe.org/3fpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fpc RCSB], [https://www.ebi.ac.uk/pdbsum/3fpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fpc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/ADH_THEBR ADH_THEBR]] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.		[[https://www.uniprot.org/uniprot/ADH_THEBR ADH_THEBR]] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/3fpc_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/3fpc_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>
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	==See Also==		==See Also==
	*[[~~Chimera of alcohol~~ dehydrogenase ~~by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH~~\|~~Chimera of alcohol~~ dehydrogenase ~~by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH~~]]		*[[Alcohol dehydrogenase\|Alcohol dehydrogenase]]
	*[[~~Chimeras of alcohol dehydrogenases\|Chimeras of alcohol dehydrogenases]]~~		*[[Alcohol dehydrogenase 3D structures\|Alcohol dehydrogenase 3D structures]]
	*[[Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase ~~by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH~~\|~~Q165E/S254K Double Mutant Chimera of alcohol~~ dehydrogenase ~~by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH]]~~
	*[[Tetrameric alcohol dehydrogenases\|Tetrameric alcohol dehydrogenases]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Enthi]]		[[Category: Enthi]]
			[[Category: Large Structures]]
	[[Category: Burstein, Y]]		[[Category: Burstein, Y]]
	[[Category: Felix, F]]		[[Category: Felix, F]]

OCA at 06:47, 1 November 2017

2017-11-01T06:47:06Z

← Older revision		Revision as of 06:47, 1 November 2017
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	==See Also==		==See Also==
	*[[Alcohol dehydrogenase\|Alcohol dehydrogenase]]
	*[[Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH\|Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH]]		*[[Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH\|Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH]]
	*[[Chimeras of alcohol dehydrogenases\|Chimeras of alcohol dehydrogenases]]		*[[Chimeras of alcohol dehydrogenases\|Chimeras of alcohol dehydrogenases]]

OCA at 11:31, 7 October 2017

2017-10-07T11:31:09Z

← Older revision		Revision as of 11:31, 7 October 2017
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	==Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH==		==Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH==
	<StructureSection load='3fpc' size='340' side='right' caption='[[3fpc]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='3fpc' size='340' side='right' caption='[[3fpc]], [[Resolution\|resolution]] 1.40Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ADH1, ADH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5759 ENTHI])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ADH1, ADH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5759 ENTHI])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] </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=3fpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fpc OCA], [http://pdbe.org/3fpc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fpc RCSB], [http://www.ebi.ac.uk/pdbsum/3fpc 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=3fpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fpc OCA], [http://pdbe.org/3fpc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fpc RCSB], [http://www.ebi.ac.uk/pdbsum/3fpc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fpc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 09:00, 9 February 2016

2016-02-09T09:00:27Z

← Older revision		Revision as of 09:00, 9 February 2016
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ADH1, ADH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5759 ENTHI])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ADH1, ADH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5759 ENTHI])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] </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=3fpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fpc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fpc RCSB], [http://www.ebi.ac.uk/pdbsum/3fpc 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=3fpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fpc OCA], [http://pdbe.org/3fpc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fpc RCSB], [http://www.ebi.ac.uk/pdbsum/3fpc PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3fpc 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 3fpc" style="background-color:#fffaf0;"></div>

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

OCA at 05:53, 25 December 2014

2014-12-25T05:53:00Z

← Older revision		Revision as of 05:53, 25 December 2014
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	~~{{STRUCTURE_3fpc\| PDB=3fpc \| SCENE= }}~~		==Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH==
	===Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH===		<StructureSection load='3fpc' size='340' side='right' caption='[[3fpc]], [[Resolution\|resolution]] 1.40Å' scene=''>
	~~{{ABSTRACT_PUBMED_20102159}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[3fpc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Enthi Enthi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FPC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FPC FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3fpl\|3fpl]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ADH1, ADH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5759 ENTHI])</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] </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=3fpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fpc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fpc RCSB], [http://www.ebi.ac.uk/pdbsum/3fpc PDBsum]</span></td></tr>
			</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/ADH_THEBR ADH_THEBR]] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.
			== 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/fp/3fpc_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 cofactor-binding domains (residues 153-295) of the alcohol dehydrogenases from the thermophile Thermoanaerobacter brockii (TbADH), the mesophilic bacterium Clostridium beijerinckii (CbADH), and the protozoan parasite Entamoeba histolytica (EhADH1) have been exchanged. Three chimeras have been constructed. In the first chimera, the cofactor-binding domain of thermophilic TbADH was replaced with the cofactor-binding domain of its mesophilic counterpart CbADH [chimera Chi21((TCT))]. This domain exchange significantly destabilized the parent thermophilic enzyme (DeltaT(1/2) = -18 degrees C). The reverse exchange in CbADH [chimera Chi22((CTC))], however, had little effect on the thermal stability of the parent mesophilic protein. Furthermore, substituting the cofactor-binding domain of TbADH with the homologous domain of EhADH1 [chimera Chi23((TET))] substantially reduced the thermal stability of the thermophilic ADH (DeltaT(1/2) = -51 degrees C) and impeded the oligomerization of the enzyme. All three chimeric proteins and one of their site-directed mutants were crystallized, and their three-dimensional (3D) structures were determined. Comparison of the 3D structures of the chimeras and the chimeric mutant with the structures of their parent ADHs showed no significant changes to their Calpha chains, suggesting that the difference in the thermal stability of the three parent ADHs and their chimeric mutants could be due to a limited number of substitutions located at strategic positions, mainly at the oligomerization interfaces. Indeed, stabilization of the chimeras was achieved, to a significant extent, either by introduction of a proline residue at a strategic position in the major horse liver ADH-type dimerization interface (DeltaT(1/2) = 35 degrees C) or by introduction of intersubunit electrostatic interactions (DeltaT(1/2) = 6 degrees C).

	~~==Function==~~		Biochemical and Structural Properties of Chimeras Constructed by Exchange of Cofactor-Binding Domains in Alcohol Dehydrogenases from Thermophilic and Mesophilic Microorganisms.,Goihberg E, Peretz M, Tel-Or S, Dym O, Shimon L, Frolow F, Burstein Y Biochemistry. 2010 Feb 9. PMID:20102159<ref>PMID:20102159</ref>
	~~[[http://www.uniprot.org/uniprot/ADH_THEBR ADH_THEBR]]~~ Alcohol ~~dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol~~ and ~~isopropanol~~. ~~Has very low activity with primary alcohols~~, ~~such as ethanol. Under physiological conditions~~, ~~the enzyme reduces aldehydes and 2~~-~~ketones to produce secondary alcohols~~. ~~Is also active with acetaldehyde and propionaldehyde~~.

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[3fpc]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Enthi Enthi]~~. ~~Full crystallographic information is available from [http:/~~/~~oca.weizmann.ac.il/oca-bin/ocashort?id=3FPC OCA].~~		</div>

	==See Also==		==See Also==
Line 15:		Line 36:
	*[[Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH\|Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH]]		*[[Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH\|Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH]]
	*[[Tetrameric alcohol dehydrogenases\|Tetrameric alcohol dehydrogenases]]		*[[Tetrameric alcohol dehydrogenases\|Tetrameric alcohol dehydrogenases]]
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:020102159</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: Enthi]]		[[Category: Enthi]]
	[[Category: Burstein, Y.]]		[[Category: Burstein, Y]]
	[[Category: Felix, F.]]		[[Category: Felix, F]]
	[[Category: Goihberg, E.]]		[[Category: Goihberg, E]]
	[[Category: Shimon, L.]]		[[Category: Shimon, L]]
	[[Category: Bacterial alcohol dehydrogenase]]		[[Category: Bacterial alcohol dehydrogenase]]
	[[Category: Chimera]]		[[Category: Chimera]]

OCA at 05:56, 29 January 2014

2014-01-29T05:56:15Z

← Older revision		Revision as of 05:56, 29 January 2014
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	===Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH===		===Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH===
	{{ABSTRACT_PUBMED_20102159}}		{{ABSTRACT_PUBMED_20102159}}

			==Function==
			[[http://www.uniprot.org/uniprot/ADH_THEBR ADH_THEBR]] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.

	==About this Structure==		==About this Structure==
	[[3fpc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Entamoeba_histolytica Entamoeba histolytica~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FPC OCA].		[[3fpc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Enthi Enthi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FPC OCA].

	==See Also==		==See Also==
Line 14:		Line 17:

	==Reference==		==Reference==
	<ref group="xtra">PMID:020102159</ref><references group="xtra"/>		<ref group="xtra">PMID:020102159</ref><references group="xtra"/><references/>
	[[Category: ~~Entamoeba histolytica~~]]		[[Category: Enthi]]
	[[Category: Burstein, Y.]]		[[Category: Burstein, Y.]]
	[[Category: Felix, F.]]		[[Category: Felix, F.]]

OCA at 10:15, 11 March 2013

2013-03-11T10:15:57Z

← Older revision		Revision as of 10:15, 11 March 2013
Line 1:		Line 1:
	~~[[Image:3fpc.png\|left\|200px]]~~

	{{STRUCTURE_3fpc\| PDB=3fpc \| SCENE= }}		{{STRUCTURE_3fpc\| PDB=3fpc \| SCENE= }}

	===Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH===		===Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH===

	{{ABSTRACT_PUBMED_20102159}}		{{ABSTRACT_PUBMED_20102159}}

OCA at 13:21, 20 October 2012

2012-10-20T13:21:03Z

← Older revision		Revision as of 13:21, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
	[[3fpc]] is a 4 chain structure ~~of [[Alcohol dehydrogenase]]~~ with sequence from [http://en.wikipedia.org/wiki/~~Thermoanaerobacter_brockii,_entamoeba_histolytica Thermoanaerobacter brockii, entamoeba~~ histolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FPC OCA].		[[3fpc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FPC OCA].

	==See Also==		==See Also==
Line 19:		Line 19:
	==Reference==		==Reference==
	<ref group="xtra">PMID:020102159</ref><references group="xtra"/>		<ref group="xtra">PMID:020102159</ref><references group="xtra"/>
	[[Category: ~~Thermoanaerobacter brockii, entamoeba~~ histolytica]]		[[Category: Entamoeba histolytica]]
	[[Category: Burstein, Y.]]		[[Category: Burstein, Y.]]
	[[Category: Felix, F.]]		[[Category: Felix, F.]]

OCA at 10:47, 15 August 2012

2012-08-15T10:47:31Z

← Older revision		Revision as of 10:47, 15 August 2012
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	*[[Alcohol dehydrogenase\|Alcohol dehydrogenase]]		*[[Alcohol dehydrogenase\|Alcohol dehydrogenase]]
	*[[Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH\|Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH]]		*[[Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH\|Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH]]
	*[[~~Chimeres~~ of alcohol dehydrogenases\|~~Chimeres~~ of alcohol dehydrogenases]]		*[[Chimeras of alcohol dehydrogenases\|Chimeras of alcohol dehydrogenases]]
	*[[Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH\|Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH]]		*[[Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH\|Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH]]
	*[[Tetrameric alcohol dehydrogenases\|Tetrameric alcohol dehydrogenases]]		*[[Tetrameric alcohol dehydrogenases\|Tetrameric alcohol dehydrogenases]]

← Older revision		Revision as of 10:47, 15 August 2012
Line 13:		Line 13:
	*[[Alcohol dehydrogenase\|Alcohol dehydrogenase]]		*[[Alcohol dehydrogenase\|Alcohol dehydrogenase]]
	*[[Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH\|Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH]]		*[[Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH\|Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH]]
	*[[~~Chimeres~~ of alcohol dehydrogenases\|~~Chimeres~~ of alcohol dehydrogenases]]		*[[Chimeras of alcohol dehydrogenases\|Chimeras of alcohol dehydrogenases]]
	*[[Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH\|Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH]]		*[[Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH\|Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH]]
	*[[Tetrameric alcohol dehydrogenases\|Tetrameric alcohol dehydrogenases]]		*[[Tetrameric alcohol dehydrogenases\|Tetrameric alcohol dehydrogenases]]