1wzg - Revision history

OCA at 13:35, 13 March 2024

OCA — Wed, 13 Mar 2024 13:35:30 GMT

←Older revision		Revision as of 13:35, 13 March 2024
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	<StructureSection load='1wzg' size='340' side='right'caption='[[1wzg]], [[Resolution\|resolution]] 1.75Å' scene=''>		<StructureSection load='1wzg' size='340' side='right'caption='[[1wzg]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1wzg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacillus_diphtheriae"_kruse_in_flugge_1886 "bacillus~~ diphtheriae~~" kruse in flugge 1886~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WZG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1wzg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WZG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YOM:2,2-[1,2-PHENYLENEBIS(NITRILOMETHYLIDYNE)]BIS[PHENOLATO]](2-)-N,N,O,O]-IRON'>YOM</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]] 1.75Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1iw0\|1iw0]], [[1iw1\|1iw1]], [[1v8x\|1v8x]], [[1wzd\|1wzd]], [[1wzf\|1wzf]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YOM:2,2-[1,2-PHENYLENEBIS(NITRILOMETHYLIDYNE)]BIS[PHENOLATO]](2-)-N,N,O,O]-IRON'>YOM</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </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=1wzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wzg OCA], [https://pdbe.org/1wzg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wzg RCSB], [https://www.ebi.ac.uk/pdbsum/1wzg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wzg 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=1wzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wzg OCA], [https://pdbe.org/1wzg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wzg RCSB], [https://www.ebi.ac.uk/pdbsum/1wzg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wzg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/HMUO_CORDI HMUO_CORDI]] Allows the bacteria to use the host heme as an iron source. Involved in the oxidation of heme and subsequent release of iron from the heme moiety.	+	[https://www.uniprot.org/uniprot/HMUO_CORDI HMUO_CORDI] Allows the bacteria to use the host heme as an iron source. Involved in the oxidation of heme and subsequent release of iron from the heme moiety.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=1wzg 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=1wzg ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Protein-to-protein electron transfer (ET) is a critical process in biological chemistry for which fundamental understanding is expected to provide a wealth of applications in biotechnology. Investigations of protein-protein ET systems in reductive activation of artificial cofactors introduced into proteins remains particularly challenging because of the complexity of interactions between the cofactor and the system contributing to ET. In this work, we construct an artificial protein-protein ET system, using heme oxygenase (HO), which is known to catalyze the conversion of heme to biliverdin. HO uses electrons provided from NADPH/cytochrome P450 reductase (CPR) through protein-protein complex formation during the enzymatic reaction. We report that a Fe(III)(Schiff-base), in the place of the active-site heme prosthetic group of HO, can be reduced by NADPH/CPR. The crystal structure of the Fe(10-CH(2)CH(2)COOH-Schiff-base).HO composite indicates the presence of a hydrogen bond between the propionic acid carboxyl group and Arg-177 of HO. Furthermore, the ET rate from NADPH/CPR to the composite is 3.5-fold faster than that of Fe(Schiff-base).HO, although the redox potential of Fe(10-CH(2)CH(2)COOH-Schiff-base).HO (-79 mV vs. NHE) is lower than that of Fe(Schiff-base).HO (+15 mV vs. NHE), where NHE is normal hydrogen electrode. This work describes a synthetic metal complex activated by means of a protein-protein ET system, which has not previously been reported. Moreover, the result suggests the importance of the hydrogen bond for the ET reaction of HO. Our Fe(Schiff-base).HO composite model system may provide insights with regard to design of ET biosystems for sensors, catalysts, and electronics devices.
-
-	Design of metal cofactors activated by a protein-protein electron transfer system.,Ueno T, Yokoi N, Unno M, Matsui T, Tokita Y, Yamada M, Ikeda-Saito M, Nakajima H, Watanabe Y Proc Natl Acad Sci U S A. 2006 Jun 20;103(25):9416-21. Epub 2006 Jun 12. PMID:16769893<ref>PMID:16769893</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1wzg" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Heme oxygenase 3D structures\|Heme oxygenase 3D structures]]		*[[Heme oxygenase 3D structures\|Heme oxygenase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus~~ diphtheriae ~~kruse in flugge 1886]]~~	+	[[Category: Corynebacterium diphtheriae]]
-	~~[[Category: Heme oxygenase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ikeda-Saito, M]]	+	[[Category: Ikeda-Saito M]]
-	[[Category: Ueno, T]]	+	[[Category: Ueno T]]
-	[[Category: Unno, M]]	+	[[Category: Unno M]]
-	[[Category: Watanabe, Y]]	+	[[Category: Watanabe Y]]
-	[[Category: Yokoi, N]]	+	[[Category: Yokoi N]]
-	~~[[Category: Artificial metalloprotein]]~~	+
-	~~[[Category: Electron-transfer]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Salophen~~]]	+

OCA at 16:30, 27 October 2021

OCA — Wed, 27 Oct 2021 16:30:54 GMT

←Older revision		Revision as of 16:30, 27 October 2021
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	<StructureSection load='1wzg' size='340' side='right'caption='[[1wzg]], [[Resolution\|resolution]] 1.75Å' scene=''>		<StructureSection load='1wzg' size='340' side='right'caption='[[1wzg]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1wzg]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacillus_diphtheriae"_kruse_in_flugge_1886 "bacillus diphtheriae" kruse in flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1WZG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1wzg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_diphtheriae"_kruse_in_flugge_1886 "bacillus diphtheriae" kruse in flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WZG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YOM:2,2-[1,2-PHENYLENEBIS(NITRILOMETHYLIDYNE)]BIS[PHENOLATO]](2-)-N,N,O,O]-IRON'>YOM</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YOM:2,2-[1,2-PHENYLENEBIS(NITRILOMETHYLIDYNE)]BIS[PHENOLATO]](2-)-N,N,O,O]-IRON'>YOM</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1iw0\|1iw0]], [[1iw1\|1iw1]], [[1v8x\|1v8x]], [[1wzd\|1wzd]], [[1wzf\|1wzf]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1iw0\|1iw0]], [[1iw1\|1iw1]], [[1v8x\|1v8x]], [[1wzd\|1wzd]], [[1wzf\|1wzf]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </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=1wzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wzg OCA], [~~http~~://pdbe.org/1wzg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1wzg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1wzg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1wzg 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=1wzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wzg OCA], [https://pdbe.org/1wzg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wzg RCSB], [https://www.ebi.ac.uk/pdbsum/1wzg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wzg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/HMUO_CORDI HMUO_CORDI]] Allows the bacteria to use the host heme as an iron source. Involved in the oxidation of heme and subsequent release of iron from the heme moiety.	+	[[https://www.uniprot.org/uniprot/HMUO_CORDI HMUO_CORDI]] Allows the bacteria to use the host heme as an iron source. Involved in the oxidation of heme and subsequent release of iron from the heme moiety.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 17:54, 22 January 2020

OCA — Wed, 22 Jan 2020 17:54:55 GMT

←Older revision		Revision as of 17:54, 22 January 2020
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	==Crystal Structure Of An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme oxygenase==		==Crystal Structure Of An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme oxygenase==
-	<StructureSection load='1wzg' size='340' side='right' caption='[[1wzg]], [[Resolution\|resolution]] 1.75Å' scene=''>	+	<StructureSection load='1wzg' size='340' side='right'caption='[[1wzg]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1wzg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_diphtheriae"_kruse_in_flugge_1886 "bacillus diphtheriae" kruse in flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WZG FirstGlance]. <br>		<table><tr><td colspan='2'>[[1wzg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_diphtheriae"_kruse_in_flugge_1886 "bacillus diphtheriae" kruse in flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WZG FirstGlance]. <br>
Line 32:		Line 32:

	==See Also==		==See Also==
-	*[[Heme oxygenase\|Heme oxygenase]]	+	*[[Heme oxygenase 3D structures\|Heme oxygenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Bacillus diphtheriae kruse in flugge 1886]]		[[Category: Bacillus diphtheriae kruse in flugge 1886]]
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
		+	[[Category: Large Structures]]
	[[Category: Ikeda-Saito, M]]		[[Category: Ikeda-Saito, M]]
	[[Category: Ueno, T]]		[[Category: Ueno, T]]

OCA at 16:37, 11 April 2018

OCA — Wed, 11 Apr 2018 16:37:11 GMT

←Older revision		Revision as of 16:37, 11 April 2018
Line 1:		Line 1:
		+
	==Crystal Structure Of An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme oxygenase==		==Crystal Structure Of An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme oxygenase==
	<StructureSection load='1wzg' size='340' side='right' caption='[[1wzg]], [[Resolution\|resolution]] 1.75Å' scene=''>		<StructureSection load='1wzg' size='340' side='right' caption='[[1wzg]], [[Resolution\|resolution]] 1.75Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1iw0\|1iw0]], [[1iw1\|1iw1]], [[1v8x\|1v8x]], [[1wzd\|1wzd]], [[1wzf\|1wzf]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1iw0\|1iw0]], [[1iw1\|1iw1]], [[1v8x\|1v8x]], [[1wzd\|1wzd]], [[1wzf\|1wzf]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </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=1wzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wzg OCA], [http://pdbe.org/1wzg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wzg RCSB], [http://www.ebi.ac.uk/pdbsum/1wzg 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=1wzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wzg OCA], [http://pdbe.org/1wzg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wzg RCSB], [http://www.ebi.ac.uk/pdbsum/1wzg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wzg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wz/1wzg_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wz/1wzg_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>
	</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=1wzg ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 09:29, 11 September 2015

OCA — Fri, 11 Sep 2015 09:29:34 GMT

←Older revision		Revision as of 09:29, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1wzg' size='340' side='right' caption='[[1wzg]], [[Resolution\|resolution]] 1.75Å' scene=''>		<StructureSection load='1wzg' size='340' side='right' caption='[[1wzg]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1wzg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Corynebacterium_diphtheriae Corynebacterium~~ diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WZG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1wzg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_diphtheriae"_kruse_in_flugge_1886 "bacillus diphtheriae" kruse in flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WZG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YOM:2,2-[1,2-PHENYLENEBIS(NITRILOMETHYLIDYNE)]BIS[PHENOLATO]](2-)-N,N,O,O]-IRON'>YOM</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YOM:2,2-[1,2-PHENYLENEBIS(NITRILOMETHYLIDYNE)]BIS[PHENOLATO]](2-)-N,N,O,O]-IRON'>YOM</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1iw0\|1iw0]], [[1iw1\|1iw1]], [[1v8x\|1v8x]], [[1wzd\|1wzd]], [[1wzf\|1wzf]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1iw0\|1iw0]], [[1iw1\|1iw1]], [[1v8x\|1v8x]], [[1wzd\|1wzd]], [[1wzf\|1wzf]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </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=1wzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wzg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wzg RCSB], [http://www.ebi.ac.uk/pdbsum/1wzg 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=1wzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wzg OCA], [http://pdbe.org/1wzg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wzg RCSB], [http://www.ebi.ac.uk/pdbsum/1wzg 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 1wzg" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Corynebacterium~~ diphtheriae]]	+	[[Category: Bacillus diphtheriae kruse in flugge 1886]]
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
	[[Category: Ikeda-Saito, M]]		[[Category: Ikeda-Saito, M]]

OCA at 14:31, 25 December 2014

OCA — Thu, 25 Dec 2014 14:31:13 GMT

←Older revision		Revision as of 14:31, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1wzg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WZG FirstGlance]. <br>		<table><tr><td colspan='2'>[[1wzg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WZG FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YOM:2,2-[1,2-PHENYLENEBIS(NITRILOMETHYLIDYNE)]BIS[PHENOLATO]](2-)-N,N,O,O]-IRON'>YOM</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YOM:2,2-[1,2-PHENYLENEBIS(NITRILOMETHYLIDYNE)]BIS[PHENOLATO]](2-)-N,N,O,O]-IRON'>YOM</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1iw0\|1iw0]], [[1iw1\|1iw1]], [[1v8x\|1v8x]], [[1wzd\|1wzd]], [[1wzf\|1wzf]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1iw0\|1iw0]], [[1iw1\|1iw1]], [[1v8x\|1v8x]], [[1wzd\|1wzd]], [[1wzf\|1wzf]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </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=1wzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wzg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wzg RCSB], [http://www.ebi.ac.uk/pdbsum/1wzg 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=1wzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wzg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wzg RCSB], [http://www.ebi.ac.uk/pdbsum/1wzg PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HMUO_CORDI HMUO_CORDI]] Allows the bacteria to use the host heme as an iron source. Involved in the oxidation of heme and subsequent release of iron from the heme moiety.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 37:
	[[Category: Corynebacterium diphtheriae]]		[[Category: Corynebacterium diphtheriae]]
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
-	[[Category: Ikeda-Saito, M.]]	+	[[Category: Ikeda-Saito, M]]
-	[[Category: Ueno, T.]]	+	[[Category: Ueno, T]]
-	[[Category: Unno, M.]]	+	[[Category: Unno, M]]
-	[[Category: Watanabe, Y.]]	+	[[Category: Watanabe, Y]]
-	[[Category: Yokoi, N.]]	+	[[Category: Yokoi, N]]
	[[Category: Artificial metalloprotein]]		[[Category: Artificial metalloprotein]]
	[[Category: Electron-transfer]]		[[Category: Electron-transfer]]
-	[[Category: Heme oxygenase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Salophen]]		[[Category: Salophen]]

OCA at 23:34, 28 September 2014

OCA — Sun, 28 Sep 2014 23:34:07 GMT

←Older revision		Revision as of 23:34, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1wzg.~~png~~\|~~left~~\|200px]]	+	==Crystal Structure Of An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme oxygenase==
		+	<StructureSection load='1wzg' size='340' side='right' caption='[[1wzg]], [[Resolution\|resolution]] 1.75Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1wzg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WZG FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=YOM:2,2-[1,2-PHENYLENEBIS(NITRILOMETHYLIDYNE)]BIS[PHENOLATO]](2-)-N,N,O,O]-IRON'>YOM</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1iw0\|1iw0]], [[1iw1\|1iw1]], [[1v8x\|1v8x]], [[1wzd\|1wzd]], [[1wzf\|1wzf]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </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=1wzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wzg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wzg RCSB], [http://www.ebi.ac.uk/pdbsum/1wzg 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/wz/1wzg_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 ==
		+	Protein-to-protein electron transfer (ET) is a critical process in biological chemistry for which fundamental understanding is expected to provide a wealth of applications in biotechnology. Investigations of protein-protein ET systems in reductive activation of artificial cofactors introduced into proteins remains particularly challenging because of the complexity of interactions between the cofactor and the system contributing to ET. In this work, we construct an artificial protein-protein ET system, using heme oxygenase (HO), which is known to catalyze the conversion of heme to biliverdin. HO uses electrons provided from NADPH/cytochrome P450 reductase (CPR) through protein-protein complex formation during the enzymatic reaction. We report that a Fe(III)(Schiff-base), in the place of the active-site heme prosthetic group of HO, can be reduced by NADPH/CPR. The crystal structure of the Fe(10-CH(2)CH(2)COOH-Schiff-base).HO composite indicates the presence of a hydrogen bond between the propionic acid carboxyl group and Arg-177 of HO. Furthermore, the ET rate from NADPH/CPR to the composite is 3.5-fold faster than that of Fe(Schiff-base).HO, although the redox potential of Fe(10-CH(2)CH(2)COOH-Schiff-base).HO (-79 mV vs. NHE) is lower than that of Fe(Schiff-base).HO (+15 mV vs. NHE), where NHE is normal hydrogen electrode. This work describes a synthetic metal complex activated by means of a protein-protein ET system, which has not previously been reported. Moreover, the result suggests the importance of the hydrogen bond for the ET reaction of HO. Our Fe(Schiff-base).HO composite model system may provide insights with regard to design of ET biosystems for sensors, catalysts, and electronics devices.

-	~~{{STRUCTURE_1wzg\| PDB=1wzg \| SCENE= }}~~	+	Design of metal cofactors activated by a protein-protein electron transfer system.,Ueno T, Yokoi N, Unno M, Matsui T, Tokita Y, Yamada M, Ikeda-Saito M, Nakajima H, Watanabe Y Proc Natl Acad Sci U S A. 2006 Jun 20;103(25):9416-21. Epub 2006 Jun 12. PMID:16769893<ref>PMID:16769893</ref>

-	~~===Crystal Structure Of An Artificial Metalloprotein: Fe(Salophen)~~/~~Wild Type Heme oxygenase===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_16769893}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1wzg]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1WZG OCA].~~	+

	==See Also==		==See Also==
	*[[Heme oxygenase\|Heme oxygenase]]		*[[Heme oxygenase\|Heme oxygenase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:016769893<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Corynebacterium diphtheriae]]		[[Category: Corynebacterium diphtheriae]]
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]

OCA at 17:51, 20 October 2012

OCA — Sat, 20 Oct 2012 17:51:00 GMT

←Older revision		Revision as of 17:51, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1wzg]] is a 2 chain structure ~~of [[Heme oxygenase]]~~ with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZG OCA].	+	[[1wzg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZG OCA].

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

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

OCA — Fri, 27 Jul 2012 02:12:01 GMT

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

←Older revision

Revision as of 02:12, 27 July 2012

OCA at 02:12, 27 July 2012

OCA — Fri, 27 Jul 2012 02:12:00 GMT

←Older revision		Revision as of 02:12, 27 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1wzg.png\|left\|200px]]		[[Image:1wzg.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1wzg", 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_1wzg\| PDB=1wzg \| SCENE= }}		{{STRUCTURE_1wzg\| PDB=1wzg \| SCENE= }}

	===Crystal Structure Of An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme oxygenase===		===Crystal Structure Of An Artificial Metalloprotein: Fe(Salophen)/Wild Type Heme oxygenase===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_16769893}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 16769893 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_16769893}}		{{ABSTRACT_PUBMED_16769893}}

	==About this Structure==		==About this Structure==
-	~~1WZG~~ is a 2 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZG OCA].	+	[[1wzg]] is a 2 chain structure of [[Heme oxygenase]] with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZG OCA].
		+
		+	==See Also==
		+	*[[Heme oxygenase\|Heme oxygenase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~16769893~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:016769893</ref><references group="xtra"/>
	[[Category: Corynebacterium diphtheriae]]		[[Category: Corynebacterium diphtheriae]]
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
Line 34:		Line 25:
	[[Category: Electron-transfer]]		[[Category: Electron-transfer]]
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
-	[[Category: ~~Metal~~]]	+	[[Category: Oxidoreductase]]
	[[Category: Salophen]]		[[Category: Salophen]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 18:46:20 2009''