1kfy - Revision history

OCA at 08:57, 16 August 2023

OCA — Wed, 16 Aug 2023 08:57:55 GMT

←Older revision		Revision as of 08:57, 16 August 2023
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	<StructureSection load='1kfy' size='340' side='right'caption='[[1kfy]], [[Resolution\|resolution]] 3.60Å' scene=''>		<StructureSection load='1kfy' size='340' side='right'caption='[[1kfy]], [[Resolution\|resolution]] 3.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1kfy]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacillus_coli"_migula_1895 "bacillus~~ coli~~" migula 1895~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1kfy]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFY FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BRS:2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL'>BRS</scene>, <scene name='pdbligand=CE1:O-DODECANYL+OCTAETHYLENE+GLYCOL'>CE1</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 3.6Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fum\|1fum]], [[1kf6\|1kf6]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BRS:2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL'>BRS</scene>, <scene name='pdbligand=CE1:O-DODECANYL+OCTAETHYLENE+GLYCOL'>CE1</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] </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=1kfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfy OCA], [https://pdbe.org/1kfy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfy RCSB], [https://www.ebi.ac.uk/pdbsum/1kfy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfy 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=1kfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfy OCA], [https://pdbe.org/1kfy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfy RCSB], [https://www.ebi.ac.uk/pdbsum/1kfy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfy ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/FRDD_ECOLI FRDD_ECOLI]] Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.[HAMAP-Rule:MF_00709] [[https://www.uniprot.org/uniprot/FRDA_ECOLI FRDA_ECOLI]] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. [[https://www.uniprot.org/uniprot/FRDC_ECOLI FRDC_ECOLI]] Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.[HAMAP-Rule:MF_00708] [[https://www.uniprot.org/uniprot/FRDB_ECOLI FRDB_ECOLI]] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.	+	[https://www.uniprot.org/uniprot/FRDA_ECOLI FRDA_ECOLI] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus~~ coli ~~migula 1895~~]]	+	[[Category: Escherichia coli]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Succinate dehydrogenase]]~~	+	[[Category: Cecchini G]]
-	[[Category: Cecchini, G]]	+	[[Category: Croal LR]]
-	[[Category: Croal~~, L R~~]]	+	[[Category: Iverson TM]]
-	[[Category: Iverson~~, T M~~]]	+	[[Category: Luna-Chavez C]]
-	[[Category: Luna-Chavez, C]]	+	[[Category: Rees DC]]
-	[[Category: Rees~~, D C]]~~	+
-	~~[[Category: Fumarate reductase]]~~	+
-	~~[[Category: Membrane protein]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Quinol]]~~	+
-	~~[[Category: Quinone]]~~	+
-	~~[[Category: Respiration~~]]	+

OCA at 08:47, 21 April 2021

OCA — Wed, 21 Apr 2021 08:47:46 GMT

←Older revision		Revision as of 08:47, 21 April 2021
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	<StructureSection load='1kfy' size='340' side='right'caption='[[1kfy]], [[Resolution\|resolution]] 3.60Å' scene=''>		<StructureSection load='1kfy' size='340' side='right'caption='[[1kfy]], [[Resolution\|resolution]] 3.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1kfy]] is a 8 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFY OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1KFY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1kfy]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFY FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BRS:2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL'>BRS</scene>, <scene name='pdbligand=CE1:O-DODECANYL+OCTAETHYLENE+GLYCOL'>CE1</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BRS:2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL'>BRS</scene>, <scene name='pdbligand=CE1:O-DODECANYL+OCTAETHYLENE+GLYCOL'>CE1</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fum\|1fum]], [[1kf6\|1kf6]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fum\|1fum]], [[1kf6\|1kf6]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] </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=1kfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfy OCA], [~~http~~://pdbe.org/1kfy PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1kfy RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1kfy PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfy 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=1kfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfy OCA], [https://pdbe.org/1kfy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfy RCSB], [https://www.ebi.ac.uk/pdbsum/1kfy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfy ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/FRDD_ECOLI FRDD_ECOLI]] Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.[HAMAP-Rule:MF_00709] [[~~http~~://www.uniprot.org/uniprot/FRDA_ECOLI FRDA_ECOLI]] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. [[~~http~~://www.uniprot.org/uniprot/FRDC_ECOLI FRDC_ECOLI]] Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.[HAMAP-Rule:MF_00708] [[~~http~~://www.uniprot.org/uniprot/FRDB_ECOLI FRDB_ECOLI]] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.	+	[[https://www.uniprot.org/uniprot/FRDD_ECOLI FRDD_ECOLI]] Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.[HAMAP-Rule:MF_00709] [[https://www.uniprot.org/uniprot/FRDA_ECOLI FRDA_ECOLI]] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. [[https://www.uniprot.org/uniprot/FRDC_ECOLI FRDC_ECOLI]] Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.[HAMAP-Rule:MF_00708] [[https://www.uniprot.org/uniprot/FRDB_ECOLI FRDB_ECOLI]] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 13:19, 17 July 2019

OCA — Wed, 17 Jul 2019 13:19:23 GMT

←Older revision		Revision as of 13:19, 17 July 2019
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	==QUINOL-FUMARATE REDUCTASE WITH QUINOL INHIBITOR 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL==		==QUINOL-FUMARATE REDUCTASE WITH QUINOL INHIBITOR 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL==
-	<StructureSection load='1kfy' size='340' side='right' caption='[[1kfy]], [[Resolution\|resolution]] 3.60Å' scene=''>	+	<StructureSection load='1kfy' size='340' side='right'caption='[[1kfy]], [[Resolution\|resolution]] 3.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1kfy]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFY FirstGlance]. <br>		<table><tr><td colspan='2'>[[1kfy]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFY FirstGlance]. <br>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kf/1kfy_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kf/1kfy_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 35:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Bacillus coli migula 1895]]		[[Category: Bacillus coli migula 1895]]
		+	[[Category: Large Structures]]
	[[Category: Succinate dehydrogenase]]		[[Category: Succinate dehydrogenase]]
	[[Category: Cecchini, G]]		[[Category: Cecchini, G]]

OCA at 07:33, 11 October 2017

OCA — Wed, 11 Oct 2017 07:33:24 GMT

←Older revision		Revision as of 07:33, 11 October 2017
Line 1:		Line 1:
		+
	==QUINOL-FUMARATE REDUCTASE WITH QUINOL INHIBITOR 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL==		==QUINOL-FUMARATE REDUCTASE WITH QUINOL INHIBITOR 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL==
	<StructureSection load='1kfy' size='340' side='right' caption='[[1kfy]], [[Resolution\|resolution]] 3.60Å' scene=''>		<StructureSection load='1kfy' size='340' side='right' caption='[[1kfy]], [[Resolution\|resolution]] 3.60Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fum\|1fum]], [[1kf6\|1kf6]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fum\|1fum]], [[1kf6\|1kf6]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] </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=1kfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfy OCA], [http://pdbe.org/1kfy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kfy RCSB], [http://www.ebi.ac.uk/pdbsum/1kfy 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=1kfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfy OCA], [http://pdbe.org/1kfy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kfy RCSB], [http://www.ebi.ac.uk/pdbsum/1kfy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfy ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	<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=1kfy ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 16:50, 11 September 2015

OCA — Fri, 11 Sep 2015 16:50:14 GMT

←Older revision		Revision as of 16:50, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1kfy' size='340' side='right' caption='[[1kfy]], [[Resolution\|resolution]] 3.60Å' scene=''>		<StructureSection load='1kfy' size='340' side='right' caption='[[1kfy]], [[Resolution\|resolution]] 3.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1kfy]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli Escherichia~~ coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1kfy]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFY FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BRS:2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL'>BRS</scene>, <scene name='pdbligand=CE1:O-DODECANYL+OCTAETHYLENE+GLYCOL'>CE1</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BRS:2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL'>BRS</scene>, <scene name='pdbligand=CE1:O-DODECANYL+OCTAETHYLENE+GLYCOL'>CE1</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fum\|1fum]], [[1kf6\|1kf6]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fum\|1fum]], [[1kf6\|1kf6]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] </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=1kfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kfy RCSB], [http://www.ebi.ac.uk/pdbsum/1kfy 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=1kfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfy OCA], [http://pdbe.org/1kfy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kfy RCSB], [http://www.ebi.ac.uk/pdbsum/1kfy PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	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 1kfy" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Escherichia~~ coli]]	+	[[Category: Bacillus coli migula 1895]]
	[[Category: Succinate dehydrogenase]]		[[Category: Succinate dehydrogenase]]
	[[Category: Cecchini, G]]		[[Category: Cecchini, G]]

OCA at 19:14, 25 December 2014

OCA — Thu, 25 Dec 2014 19:14:05 GMT

←Older revision		Revision as of 19:14, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1kfy]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFY FirstGlance]. <br>		<table><tr><td colspan='2'>[[1kfy]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFY FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BRS:2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL'>BRS</scene>, <scene name='pdbligand=CE1:O-DODECANYL+OCTAETHYLENE+GLYCOL'>CE1</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BRS:2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL'>BRS</scene>, <scene name='pdbligand=CE1:O-DODECANYL+OCTAETHYLENE+GLYCOL'>CE1</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fum\|1fum]], [[1kf6\|1kf6]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fum\|1fum]], [[1kf6\|1kf6]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] </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=1kfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kfy RCSB], [http://www.ebi.ac.uk/pdbsum/1kfy 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=1kfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kfy RCSB], [http://www.ebi.ac.uk/pdbsum/1kfy PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FRDD_ECOLI FRDD_ECOLI]] Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.[HAMAP-Rule:MF_00709] [[http://www.uniprot.org/uniprot/FRDA_ECOLI FRDA_ECOLI]] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. [[http://www.uniprot.org/uniprot/FRDC_ECOLI FRDC_ECOLI]] Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.[HAMAP-Rule:MF_00708] [[http://www.uniprot.org/uniprot/FRDB_ECOLI FRDB_ECOLI]] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Succinate dehydrogenase]]		[[Category: Succinate dehydrogenase]]
-	[[Category: Cecchini, G.]]	+	[[Category: Cecchini, G]]
-	[[Category: Croal, L R.]]	+	[[Category: Croal, L R]]
-	[[Category: Iverson, T M.]]	+	[[Category: Iverson, T M]]
-	[[Category: Luna-Chavez, C.]]	+	[[Category: Luna-Chavez, C]]
-	[[Category: Rees, D C.]]	+	[[Category: Rees, D C]]
	[[Category: Fumarate reductase]]		[[Category: Fumarate reductase]]
	[[Category: Membrane protein]]		[[Category: Membrane protein]]
Line 43:		Line 45:
	[[Category: Quinone]]		[[Category: Quinone]]
	[[Category: Respiration]]		[[Category: Respiration]]
-	[[Category: Succinate dehydrogenase]]

OCA at 08:40, 28 September 2014

OCA — Sun, 28 Sep 2014 08:40:55 GMT

←Older revision		Revision as of 08:40, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1kfy.~~png~~\|~~left~~\|200px]]	+	==QUINOL-FUMARATE REDUCTASE WITH QUINOL INHIBITOR 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL==
		+	<StructureSection load='1kfy' size='340' side='right' caption='[[1kfy]], [[Resolution\|resolution]] 3.60Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1kfy]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFY FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BRS:2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL'>BRS</scene>, <scene name='pdbligand=CE1:O-DODECANYL+OCTAETHYLENE+GLYCOL'>CE1</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1fum\|1fum]], [[1kf6\|1kf6]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] </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=1kfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kfy RCSB], [http://www.ebi.ac.uk/pdbsum/1kfy 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/kf/1kfy_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 quinol-fumarate reductase (QFR) respiratory complex of Escherichia coli is a four-subunit integral-membrane complex that catalyzes the final step of anaerobic respiration when fumarate is the terminal electron acceptor. The membrane-soluble redox-active molecule menaquinol (MQH(2)) transfers electrons to QFR by binding directly to the membrane-spanning region. The crystal structure of QFR contains two quinone species, presumably MQH(2), bound to the transmembrane-spanning region. The binding sites for the two quinone molecules are termed Q(P) and Q(D), indicating their positions proximal (Q(P)) or distal (Q(D)) to the site of fumarate reduction in the hydrophilic flavoprotein and iron-sulfur protein subunits. It has not been established whether both of these sites are mechanistically significant. Co-crystallization studies of the E. coli QFR with the known quinol-binding site inhibitors 2-heptyl-4-hydroxyquinoline-N-oxide and 2-[1-(p-chlorophenyl)ethyl] 4,6-dinitrophenol establish that both inhibitors block the binding of MQH(2) at the Q(P) site. In the structures with the inhibitor bound at Q(P), no density is observed at Q(D), which suggests that the occupancy of this site can vary and argues against a structurally obligatory role for quinol binding to Q(D). A comparison of the Q(P) site of the E. coli enzyme with quinone-binding sites in other respiratory enzymes shows that an acidic residue is structurally conserved. This acidic residue, Glu-C29, in the E. coli enzyme may act as a proton shuttle from the quinol during enzyme turnover.

-	~~{{STRUCTURE_1kfy\| PDB=1kfy \| SCENE= }}~~	+	Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site.,Iverson TM, Luna-Chavez C, Croal LR, Cecchini G, Rees DC J Biol Chem. 2002 May 3;277(18):16124-30. Epub 2002 Feb 15. PMID:11850430<ref>PMID:11850430</ref>

-	~~===QUINOL-FUMARATE REDUCTASE WITH QUINOL INHIBITOR 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4~~,~~6-DINITRO-PHENOL===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_11850430}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1kfy]] is~~ a ~~8 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Escherichia_coli Escherichia coli]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1KFY OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:011850430<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Succinate dehydrogenase]]		[[Category: Succinate dehydrogenase]]

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

OCA — Wed, 05 Dec 2012 20:00:44 GMT

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

←Older revision

Revision as of 20:00, 5 December 2012

OCA at 20:00, 5 December 2012

OCA — Wed, 05 Dec 2012 20:00:41 GMT

←Older revision		Revision as of 20:00, 5 December 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1kfy.png\|left\|200px]]		[[Image:1kfy.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1kfy", 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_1kfy\| PDB=1kfy \| SCENE= }}		{{STRUCTURE_1kfy\| PDB=1kfy \| SCENE= }}

	===QUINOL-FUMARATE REDUCTASE WITH QUINOL INHIBITOR 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL===		===QUINOL-FUMARATE REDUCTASE WITH QUINOL INHIBITOR 2-[1-(4-CHLORO-PHENYL)-ETHYL]-4,6-DINITRO-PHENOL===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_11850430}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 11850430 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_11850430}}		{{ABSTRACT_PUBMED_11850430}}

	==About this Structure==		==About this Structure==
-	~~1KFY~~ is a 8 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFY OCA].	+	[[1kfy]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFY OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~11850430~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:011850430</ref><references group="xtra"/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Succinate dehydrogenase]]		[[Category: Succinate dehydrogenase]]
Line 38:		Line 26:
	[[Category: Respiration]]		[[Category: Respiration]]
	[[Category: Succinate dehydrogenase]]		[[Category: Succinate dehydrogenase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 2 16:16:56 2009''

OCA at 13:16, 2 April 2009

OCA — Thu, 02 Apr 2009 13:16:57 GMT

←Older revision		Revision as of 13:16, 2 April 2009
Line 33:		Line 33:
	[[Category: Fumarate reductase]]		[[Category: Fumarate reductase]]
	[[Category: Membrane protein]]		[[Category: Membrane protein]]
		+	[[Category: Oxidoreductase]]
	[[Category: Quinol]]		[[Category: Quinol]]
	[[Category: Quinone]]		[[Category: Quinone]]
Line 38:		Line 39:
	[[Category: Succinate dehydrogenase]]		[[Category: Succinate dehydrogenase]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Feb 18 04~~:10:19 2009''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 2 16:16:56 2009''