4eht - Revision history

OCA at 10:51, 13 August 2026

2026-08-13T10:51:08Z

← Older revision		Revision as of 10:51, 13 August 2026
Line 5:		Line 5:
	<table><tr><td colspan='2'>[[4eht]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile Clostridioides difficile]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EHT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4eht]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile Clostridioides difficile]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EHT FirstGlance]. <br>
	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.95Å</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]] 1.95Å</td></tr>
	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4~~</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4~~</scene></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene></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=4eht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eht OCA], [https://pdbe.org/4eht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eht RCSB], [https://www.ebi.ac.uk/pdbsum/4eht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eht 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=4eht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eht OCA], [https://pdbe.org/4eht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eht RCSB], [https://www.ebi.ac.uk/pdbsum/4eht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eht ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/HADI_CLODI HADI_CLODI] Involved in the reductive branch of L-leucine fermentation. Required for the activation of (R)-2-hydroxyisocaproyl-CoA dehydratase. The reduced activator transfers one electron to the dehydratase concomitant with hydrolysis of ATP. This protein is extremely sensitive towards oxygen.<ref>PMID:15654892</ref> <ref>PMID:22827463</ref>		[https://www.uniprot.org/uniprot/HADI_CLODI HADI_CLODI] Involved in the reductive branch of L-leucine fermentation. Required for the activation of (R)-2-hydroxyisocaproyl-CoA dehydratase. The reduced activator transfers one electron to the dehydratase concomitant with hydrolysis of ATP. This protein is extremely sensitive towards oxygen.<ref>PMID:15654892</ref> <ref>PMID:22827463</ref>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Members of the 2-hydroxyacyl-CoA dehydratase enzyme family catalyze the beta,alpha-dehydration of various CoA-esters in the fermentation of amino acids by clostridia. Abstraction of the non-acidic beta-proton of the 2-hydroxyacyl-CoA compounds is achieved by the reductive generation of ketyl radicals on the substrate, which is initiated by the transfer of an electron at low redox potentials. The highly energetic electron needed on the dehydratase is donated by a [4Fe-4S] cluster containing ATPase, termed activator. We investigated the activator of the 2-hydroxyisocaproyl-CoA dehydratase from Clostridium difficile. The activator is a homodimeric protein structurally related to acetate and sugar kinases, Hsc70 and actin, which has a [4Fe-4S] cluster bound in the dimer interface. The crystal structures of the Mg-ADP, Mg-ADPNP and nucleotide-free states of the reduced activator have been solved at 1.6 - 3.0 A resolution, allowing us to define the position of Mg2+ and water molecules in the vicinity of the nucleotides and the [4Fe-4S] cluster. The structures reveal redox- and nucleotide dependent changes agreeing with the modulation of the reduction potential of the [4Fe-4S] cluster by conformational changes. We also investigated the propensity of the activator to form a complex with its cognate dehydratase in the presence of Mg-ADP and Mg-ADPNP and together with the structural data present a refined mechanistic scheme for the ATP-dependent electron transfer between activator and dehydratase.

			On the ATP-dependent Activation of the Radical Enzyme (R)-2-Hydroxyisocaproyl-CoA Dehydratase.,Knauer SH, Buckel W, Dobbek H Biochemistry. 2012 Jul 24. PMID:22827463<ref>PMID:22827463</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 4eht" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:01, 14 March 2024

2024-03-14T15:01:47Z

← Older revision		Revision as of 15:01, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4eht]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile Clostridioides difficile]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EHT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4eht]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile Clostridioides difficile]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EHT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</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]] 1.95Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></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=4eht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eht OCA], [https://pdbe.org/4eht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eht RCSB], [https://www.ebi.ac.uk/pdbsum/4eht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eht 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=4eht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eht OCA], [https://pdbe.org/4eht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eht RCSB], [https://www.ebi.ac.uk/pdbsum/4eht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eht ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/HADI_CLODI HADI_CLODI]] Involved in the reductive branch of L-leucine fermentation. Required for the activation of (R)-2-hydroxyisocaproyl-CoA dehydratase. The reduced activator transfers one electron to the dehydratase concomitant with hydrolysis of ATP. This protein is extremely sensitive towards oxygen.<ref>PMID:15654892</ref> <ref>PMID:22827463</ref>		[https://www.uniprot.org/uniprot/HADI_CLODI HADI_CLODI] Involved in the reductive branch of L-leucine fermentation. Required for the activation of (R)-2-hydroxyisocaproyl-CoA dehydratase. The reduced activator transfers one electron to the dehydratase concomitant with hydrolysis of ATP. This protein is extremely sensitive towards oxygen.<ref>PMID:15654892</ref> <ref>PMID:22827463</ref>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Members of the 2-hydroxyacyl-CoA dehydratase enzyme family catalyze the beta,alpha-dehydration of various CoA-esters in the fermentation of amino acids by clostridia. Abstraction of the non-acidic beta-proton of the 2-hydroxyacyl-CoA compounds is achieved by the reductive generation of ketyl radicals on the substrate, which is initiated by the transfer of an electron at low redox potentials. The highly energetic electron needed on the dehydratase is donated by a [4Fe-4S] cluster containing ATPase, termed activator. We investigated the activator of the 2-hydroxyisocaproyl-CoA dehydratase from Clostridium difficile. The activator is a homodimeric protein structurally related to acetate and sugar kinases, Hsc70 and actin, which has a [4Fe-4S] cluster bound in the dimer interface. The crystal structures of the Mg-ADP, Mg-ADPNP and nucleotide-free states of the reduced activator have been solved at 1.6 - 3.0 A resolution, allowing us to define the position of Mg2+ and water molecules in the vicinity of the nucleotides and the [4Fe-4S] cluster. The structures reveal redox- and nucleotide dependent changes agreeing with the modulation of the reduction potential of the [4Fe-4S] cluster by conformational changes. We also investigated the propensity of the activator to form a complex with its cognate dehydratase in the presence of Mg-ADP and Mg-ADPNP and together with the structural data present a refined mechanistic scheme for the ATP-dependent electron transfer between activator and dehydratase.

	~~On the ATP-dependent Activation of the Radical Enzyme (R)-2-Hydroxyisocaproyl-CoA Dehydratase.,Knauer SH, Buckel W, Dobbek H Biochemistry. 2012 Jul 24. PMID:22827463<ref>PMID:22827463</ref>~~

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4eht" style="background-color:#fffaf0;"></div~~>
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:12, 28 September 2022

2022-09-28T07:12:04Z

← Older revision		Revision as of 07:12, 28 September 2022
Line 1:		Line 1:

	==Activator of the 2-Hydroxyisocaproyl-CoA dehydratase from Clostridium difficile with bound ADP==		==Activator of the 2-Hydroxyisocaproyl-CoA dehydratase from Clostridium difficile with bound ADP==
	<StructureSection load='4eht' size='340' side='right' caption='[[4eht]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='4eht' size='340' side='right'caption='[[4eht]], [[Resolution\|resolution]] 1.95Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4eht]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"bacillus_difficilis"_hall_and_o'toole_1935 "bacillus difficilis" hall and o'toole 1935~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EHT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4EHT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4eht]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile Clostridioides difficile]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EHT FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</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">[[4ehu\|4ehu]], [[4eia\|4eia]]</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=4eht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eht OCA], [https://pdbe.org/4eht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eht RCSB], [https://www.ebi.ac.uk/pdbsum/4eht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eht ProSAT]</span></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hadI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1496 "Bacillus difficilis" Hall and O'Toole 1935])</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=4eht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eht OCA], [~~http~~://pdbe.org/4eht PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4eht RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4eht PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4eht ProSAT]</span></td></tr>
	</table>		</table>
			== Function ==
			[[https://www.uniprot.org/uniprot/HADI_CLODI HADI_CLODI]] Involved in the reductive branch of L-leucine fermentation. Required for the activation of (R)-2-hydroxyisocaproyl-CoA dehydratase. The reduced activator transfers one electron to the dehydratase concomitant with hydrolysis of ATP. This protein is extremely sensitive towards oxygen.<ref>PMID:15654892</ref> <ref>PMID:22827463</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Bacillus difficilis hall and o'toole 1935~~]]		[[Category: Clostridioides difficile]]
	[[Category: ~~Dobbek, H~~]]		[[Category: Large Structures]]
	[[Category: ~~Knauer, S~~ H]]		[[Category: Dobbek H]]
	[[Category: ~~2-hydroxyisocaproyl-coa dehydratase binding]]~~		[[Category: Knauer SH]]
	~~[[Category: Actin fold]]~~
	~~[[Category: Atp/adp binding]]~~
	~~[[Category: Atpase]]~~
	~~[[Category: Electron transfer]]~~
	~~[[Category: Electron transport~~]]

OCA at 18:51, 11 August 2016

2016-08-11T18:51:11Z

← Older revision		Revision as of 18:51, 11 August 2016
Line 1:		Line 1:

	==Activator of the 2-Hydroxyisocaproyl-CoA dehydratase from Clostridium difficile with bound ADP==		==Activator of the 2-Hydroxyisocaproyl-CoA dehydratase from Clostridium difficile with bound ADP==
	<StructureSection load='4eht' size='340' side='right' caption='[[4eht]], [[Resolution\|resolution]] 1.95Å' scene=''>		<StructureSection load='4eht' size='340' side='right' caption='[[4eht]], [[Resolution\|resolution]] 1.95Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ehu\|4ehu]], [[4eia\|4eia]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ehu\|4ehu]], [[4eia\|4eia]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hadI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1496 "Bacillus difficilis" Hall and O'Toole 1935])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hadI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1496 "Bacillus difficilis" Hall and O'Toole 1935])</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=4eht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eht OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eht RCSB], [http://www.ebi.ac.uk/pdbsum/4eht 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=4eht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eht OCA], [http://pdbe.org/4eht PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4eht RCSB], [http://www.ebi.ac.uk/pdbsum/4eht PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4eht ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 16:		Line 17:
	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 4eht" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:46, 4 January 2015

2015-01-04T13:46:30Z

← Older revision		Revision as of 13:46, 4 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4eht]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_difficilis"_hall_and_o'toole_1935 "bacillus difficilis" hall and o'toole 1935]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EHT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4eht]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_difficilis"_hall_and_o'toole_1935 "bacillus difficilis" hall and o'toole 1935]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EHT FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</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">[[4ehu\|4ehu]], [[4eia\|4eia]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ehu\|4ehu]], [[4eia\|4eia]]</td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hadI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1496 "Bacillus difficilis" Hall and O'Toole 1935])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hadI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1496 "Bacillus difficilis" Hall and O'Toole 1935])</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=4eht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eht OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eht RCSB], [http://www.ebi.ac.uk/pdbsum/4eht 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=4eht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eht OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eht RCSB], [http://www.ebi.ac.uk/pdbsum/4eht PDBsum]</span></td></tr>
	<table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 21:
	</StructureSection>		</StructureSection>
	[[Category: Bacillus difficilis hall and o'toole 1935]]		[[Category: Bacillus difficilis hall and o'toole 1935]]
	[[Category: Dobbek, H.]]		[[Category: Dobbek, H]]
	[[Category: Knauer, S H.]]		[[Category: Knauer, S H]]
	[[Category: 2-hydroxyisocaproyl-coa dehydratase binding]]		[[Category: 2-hydroxyisocaproyl-coa dehydratase binding]]
	[[Category: Actin fold]]		[[Category: Actin fold]]

OCA at 06:56, 25 June 2014

2014-06-25T06:56:16Z

← Older revision		Revision as of 06:56, 25 June 2014
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	[[~~Image~~:~~4eht~~.~~png~~\|~~left~~\|~~200px~~]]		==Activator of the 2-Hydroxyisocaproyl-CoA dehydratase from Clostridium difficile with bound ADP==
			<StructureSection load='4eht' size='340' side='right' caption='[[4eht]], [[Resolution\|resolution]] 1.95Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4eht]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_difficilis"_hall_and_o'toole_1935 "bacillus difficilis" hall and o'toole 1935]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EHT FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ehu\|4ehu]], [[4eia\|4eia]]</td></tr>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hadI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1496 "Bacillus difficilis" Hall and O'Toole 1935])</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=4eht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eht OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eht RCSB], [http://www.ebi.ac.uk/pdbsum/4eht PDBsum]</span></td></tr>
			<table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Members of the 2-hydroxyacyl-CoA dehydratase enzyme family catalyze the beta,alpha-dehydration of various CoA-esters in the fermentation of amino acids by clostridia. Abstraction of the non-acidic beta-proton of the 2-hydroxyacyl-CoA compounds is achieved by the reductive generation of ketyl radicals on the substrate, which is initiated by the transfer of an electron at low redox potentials. The highly energetic electron needed on the dehydratase is donated by a [4Fe-4S] cluster containing ATPase, termed activator. We investigated the activator of the 2-hydroxyisocaproyl-CoA dehydratase from Clostridium difficile. The activator is a homodimeric protein structurally related to acetate and sugar kinases, Hsc70 and actin, which has a [4Fe-4S] cluster bound in the dimer interface. The crystal structures of the Mg-ADP, Mg-ADPNP and nucleotide-free states of the reduced activator have been solved at 1.6 - 3.0 A resolution, allowing us to define the position of Mg2+ and water molecules in the vicinity of the nucleotides and the [4Fe-4S] cluster. The structures reveal redox- and nucleotide dependent changes agreeing with the modulation of the reduction potential of the [4Fe-4S] cluster by conformational changes. We also investigated the propensity of the activator to form a complex with its cognate dehydratase in the presence of Mg-ADP and Mg-ADPNP and together with the structural data present a refined mechanistic scheme for the ATP-dependent electron transfer between activator and dehydratase.

	~~{{STRUCTURE_4eht\| PDB=4eht \| SCENE= }}~~		On the ATP-dependent Activation of the Radical Enzyme (R)-2-Hydroxyisocaproyl-CoA Dehydratase.,Knauer SH, Buckel W, Dobbek H Biochemistry. 2012 Jul 24. PMID:22827463<ref>PMID:22827463</ref>

	~~===Activator~~ of the ~~2-Hydroxyisocaproyl-CoA dehydratase from Clostridium difficile with bound ADP===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_22827463}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[4eht]] is a 2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Clostridium_difficile Clostridium difficile]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4EHT OCA].~~		</StructureSection>
			[[Category: Bacillus difficilis hall and o'toole 1935]]
	==~~Reference~~==
	<~~ref group="xtra">PMID:022827463<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: ~~Clostridium difficile~~]]
	[[Category: Dobbek, H.]]		[[Category: Dobbek, H.]]
	[[Category: Knauer, S H.]]		[[Category: Knauer, S H.]]

OCA at 05:50, 5 September 2012

2012-09-05T05:50:11Z

← Older revision		Revision as of 05:50, 5 September 2012
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	[[Image:4eht.~~jpg~~\|left\|200px]]		[[Image:4eht.png\|left\|200px]]

	{{STRUCTURE_4eht\| PDB=4eht \| SCENE= }}		{{STRUCTURE_4eht\| PDB=4eht \| SCENE= }}

OCA at 05:23, 8 August 2012

2012-08-08T05:23:18Z

← Older revision		Revision as of 05:23, 8 August 2012
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	~~'''Unreleased structure'''~~		[[Image:4eht.jpg\|left\|200px]]

	~~The entry~~ 4eht ~~is ON HOLD~~ ~~until Paper Publication~~		{{STRUCTURE_4eht\| PDB=4eht \| SCENE= }}

	~~Authors: Knauer, S.H., Dobbek, H.~~		===Activator of the 2-Hydroxyisocaproyl-CoA dehydratase from Clostridium difficile with bound ADP===

	~~Description~~: ~~Activator of the~~ 2-~~Hydroxyisocaproyl~~-~~CoA~~ dehydratase ~~from Clostridium difficile with bound ADP~~		{{ABSTRACT_PUBMED_22827463}}

			==About this Structure==
			[[4eht]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_difficile Clostridium difficile]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EHT OCA].

			==Reference==
			<ref group="xtra">PMID:022827463</ref><references group="xtra"/>
			[[Category: Clostridium difficile]]
			[[Category: Dobbek, H.]]
			[[Category: Knauer, S H.]]
			[[Category: 2-hydroxyisocaproyl-coa dehydratase binding]]
			[[Category: Actin fold]]
			[[Category: Atp/adp binding]]
			[[Category: Atpase]]
			[[Category: Electron transfer]]
			[[Category: Electron transport]]

OCA at 08:52, 25 April 2012

2012-04-25T08:52:47Z

← Older revision		Revision as of 08:52, 25 April 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4eht is ON HOLD		The entry 4eht is ON HOLD until Paper Publication

	Authors: Knauer, S.H., Dobbek, H.		Authors: Knauer, S.H., Dobbek, H.

	Description: Activator of the 2-Hydroxyisocaproyl-CoA dehydratase from Clostridium difficile with bound ADP		Description: Activator of the 2-Hydroxyisocaproyl-CoA dehydratase from Clostridium difficile with bound ADP

OCA at 07:31, 18 April 2012

2012-04-18T07:31:44Z

← Older revision		Revision as of 07:31, 18 April 2012
Line 3:		Line 3:
	The entry 4eht is ON HOLD		The entry 4eht is ON HOLD

	Authors: Knauer, SH, Dobbek, H.		Authors: Knauer, S.H., Dobbek, H.

	Description: Activator of the 2-Hydroxyisocaproyl-CoA dehydratase from Clostridium difficile with bound ADP		Description: Activator of the 2-Hydroxyisocaproyl-CoA dehydratase from Clostridium difficile with bound ADP