4e4e - Revision history

OCA at 14:52, 14 March 2024

2024-03-14T14:52:20Z

← Older revision		Revision as of 14:52, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e4e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E4E FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e4e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E4E FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 1.88Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=4e4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e4e OCA], [https://pdbe.org/4e4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e4e RCSB], [https://www.ebi.ac.uk/pdbsum/4e4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e4e 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=4e4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e4e OCA], [https://pdbe.org/4e4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e4e RCSB], [https://www.ebi.ac.uk/pdbsum/4e4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e4e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/SODM_YEAST SODM_YEAST]] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.		[https://www.uniprot.org/uniprot/SODM_YEAST SODM_YEAST] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Reduction of superoxide ( ) by manganese-containing superoxide dismutase occurs through either a "prompt protonation" pathway, or an "inner-sphere" pathway, with the latter leading to formation of an observable Mn-peroxo complex. We recently reported that wild-type (WT) manganese superoxide dismutases (MnSODs) from Saccharomyces cerevisiae and Candida albicans are more gated toward the "prompt protonation" pathway than human and bacterial MnSODs and suggested that this could result from small structural changes in the second coordination sphere of manganese. We report here that substitution of a second-sphere residue, Tyr34, by phenylalanine (Y34F) causes the MnSOD from S. cerevisiae to react exclusively through the "inner-sphere" pathway. At neutral pH, we have a surprising observation that protonation of the Mn-peroxo complex in the mutant yeast enzyme occurs through a fast pathway, leading to a putative six-coordinate Mn(3+) species, which actively oxidizes in the catalytic cycle. Upon increasing pH, the fast pathway is gradually replaced by a slow proton-transfer pathway, leading to the well-characterized five-coordinate Mn(3+). We here propose and compare two hypothetical mechanisms for the mutant yeast enzyme, differing in the structure of the Mn-peroxo complex yet both involving formation of the active six-coordinate Mn(3+) and proton transfer from a second-sphere water molecule, which has substituted for the horizontal line OH of Tyr34, to the Mn-peroxo complex. Because WT and the mutant yeast MnSOD both rest in the 2+ state and become six-coordinate when oxidized up from Mn(2+), six-coordinate Mn(3+) species could also actively function in the mechanism of WT yeast MnSODs.

	Six-coordinate manganese(3+) in catalysis by yeast manganese superoxide dismutase.,Sheng Y, Butler Gralla E, Schumacher M, Cascio D, Cabelli DE, Selverstone Valentine J Proc Natl Acad Sci U S A. 2012 Sep 4;109(36):14314-9. Epub 2012 Aug 20. PMID:22908245<ref>PMID:22908245</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4e4e" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Superoxide dismutase 3D structures\|Superoxide dismutase 3D structures]]		*[[Superoxide dismutase 3D structures\|Superoxide dismutase 3D structures]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 06:49, 28 September 2022

2022-09-28T06:49:28Z

← Older revision		Revision as of 06:49, 28 September 2022
Line 1:		Line 1:

	==Crystal Structure of the Y34F mutant of Saccharomyces cerevisiae Manganese Superoxide Dismutase==		==Crystal Structure of the Y34F mutant of Saccharomyces cerevisiae Manganese Superoxide Dismutase==
	<StructureSection load='4e4e' size='340' side='right' caption='[[4e4e]], [[Resolution\|resolution]] 1.88Å' scene=''>		<StructureSection load='4e4e' size='340' side='right'caption='[[4e4e]], [[Resolution\|resolution]] 1.88Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e4e]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Atcc_18824 Atcc 18824~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E4E OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4E4E FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e4e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E4E FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
	~~<tr~~ id~~='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class~~="~~sblockDat~~"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</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=4e4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e4e OCA], [https://pdbe.org/4e4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e4e RCSB], [https://www.ebi.ac.uk/pdbsum/4e4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e4e ProSAT]</span></td></tr>
	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b></td><td class="sblockDat">SOD2, YHR008C~~ (~~[http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]~~)~~</td></tr>~~
	~~<tr id='activity~~'>~~<td class="sblockLbl"><b>Activity:~~</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </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=4e4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e4e OCA], [~~http~~://pdbe.org/4e4e PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4e4e RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4e4e PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4e4e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/SODM_YEAST SODM_YEAST]] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.		[[https://www.uniprot.org/uniprot/SODM_YEAST SODM_YEAST]] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 20:

	==See Also==		==See Also==
	*[[Superoxide ~~Dismutase~~\|Superoxide ~~Dismutase~~]]		*[[Superoxide dismutase 3D structures\|Superoxide dismutase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Atcc 18824~~]]		[[Category: Large Structures]]
	[[Category: ~~Superoxide dismutase~~]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: Cascio, D]]		[[Category: Cascio D]]
	[[Category: Sheng, Y]]		[[Category: Sheng Y]]
	[[Category: Valentine~~, J S]]~~		[[Category: Valentine JS]]
	~~[[Category: Mn superoxide dismutase]]~~
	~~[[Category: Oxidoreductase~~]]

OCA at 04:39, 5 August 2016

2016-08-05T04:39:46Z

← Older revision		Revision as of 04:39, 5 August 2016
Line 1:		Line 1:

	==Crystal Structure of the Y34F mutant of Saccharomyces cerevisiae Manganese Superoxide Dismutase==		==Crystal Structure of the Y34F mutant of Saccharomyces cerevisiae Manganese Superoxide Dismutase==
	<StructureSection load='4e4e' size='340' side='right' caption='[[4e4e]], [[Resolution\|resolution]] 1.88Å' scene=''>		<StructureSection load='4e4e' size='340' side='right' caption='[[4e4e]], [[Resolution\|resolution]] 1.88Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e4e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Saccharomyces_cerevisiae Saccharomyces cerevisiae~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E4E FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e4e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E4E FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SOD2, YHR008C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ~~Saccharomyces cerevisiae~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SOD2, YHR008C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </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=4e4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e4e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e4e RCSB], [http://www.ebi.ac.uk/pdbsum/4e4e 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=4e4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e4e OCA], [http://pdbe.org/4e4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e4e RCSB], [http://www.ebi.ac.uk/pdbsum/4e4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e4e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 4e4e" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 26:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Saccharomyces cerevisiae~~]]		[[Category: Atcc 18824]]
	[[Category: Superoxide dismutase]]		[[Category: Superoxide dismutase]]
	[[Category: Cascio, D]]		[[Category: Cascio, D]]

OCA at 15:51, 25 December 2014

2014-12-25T15:51:57Z

← Older revision		Revision as of 15:51, 25 December 2014
Line 1:		Line 1:
	[[~~Image~~:~~4e4e~~.~~png~~\|~~left~~\|~~200px~~]]		==Crystal Structure of the Y34F mutant of Saccharomyces cerevisiae Manganese Superoxide Dismutase==
			<StructureSection load='4e4e' size='340' side='right' caption='[[4e4e]], [[Resolution\|resolution]] 1.88Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[4e4e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E4E FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
			<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SOD2, YHR008C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </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=4e4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e4e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e4e RCSB], [http://www.ebi.ac.uk/pdbsum/4e4e PDBsum]</span></td></tr>
			</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/SODM_YEAST SODM_YEAST]] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Reduction of superoxide ( ) by manganese-containing superoxide dismutase occurs through either a "prompt protonation" pathway, or an "inner-sphere" pathway, with the latter leading to formation of an observable Mn-peroxo complex. We recently reported that wild-type (WT) manganese superoxide dismutases (MnSODs) from Saccharomyces cerevisiae and Candida albicans are more gated toward the "prompt protonation" pathway than human and bacterial MnSODs and suggested that this could result from small structural changes in the second coordination sphere of manganese. We report here that substitution of a second-sphere residue, Tyr34, by phenylalanine (Y34F) causes the MnSOD from S. cerevisiae to react exclusively through the "inner-sphere" pathway. At neutral pH, we have a surprising observation that protonation of the Mn-peroxo complex in the mutant yeast enzyme occurs through a fast pathway, leading to a putative six-coordinate Mn(3+) species, which actively oxidizes in the catalytic cycle. Upon increasing pH, the fast pathway is gradually replaced by a slow proton-transfer pathway, leading to the well-characterized five-coordinate Mn(3+). We here propose and compare two hypothetical mechanisms for the mutant yeast enzyme, differing in the structure of the Mn-peroxo complex yet both involving formation of the active six-coordinate Mn(3+) and proton transfer from a second-sphere water molecule, which has substituted for the horizontal line OH of Tyr34, to the Mn-peroxo complex. Because WT and the mutant yeast MnSOD both rest in the 2+ state and become six-coordinate when oxidized up from Mn(2+), six-coordinate Mn(3+) species could also actively function in the mechanism of WT yeast MnSODs.

	~~{{STRUCTURE_4e4e\| PDB=4e4e \| SCENE= }}~~		Six-coordinate manganese(3+) in catalysis by yeast manganese superoxide dismutase.,Sheng Y, Butler Gralla E, Schumacher M, Cascio D, Cabelli DE, Selverstone Valentine J Proc Natl Acad Sci U S A. 2012 Sep 4;109(36):14314-9. Epub 2012 Aug 20. PMID:22908245<ref>PMID:22908245</ref>

	~~===Crystal Structure~~ of the ~~Y34F mutant~~ of ~~Saccharomyces cerevisiae Manganese Superoxide Dismutase===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	~~{{ABSTRACT_PUBMED_22908245}}~~		==See Also==
			*[[Superoxide Dismutase\|Superoxide Dismutase]]
	==~~About this Structure~~==		== References ==
	[[~~4e4e~~]] ~~is a 4 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E4E OCA].~~		<references/>
			__TOC__
			</StructureSection>
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: Superoxide dismutase]]		[[Category: Superoxide dismutase]]
	[[Category: Cascio, D.]]		[[Category: Cascio, D]]
	[[Category: Sheng, Y.]]		[[Category: Sheng, Y]]
	[[Category: Valentine, J S.]]		[[Category: Valentine, J S]]
	[[Category: Mn superoxide dismutase]]		[[Category: Mn superoxide dismutase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 20:32, 26 September 2012

2012-09-26T20:32:55Z

← Older revision		Revision as of 20:32, 26 September 2012
Line 1:		Line 1:
	[[Image:4e4e.~~jpg~~\|left\|200px]]		[[Image:4e4e.png\|left\|200px]]

	{{STRUCTURE_4e4e\| PDB=4e4e \| SCENE= }}		{{STRUCTURE_4e4e\| PDB=4e4e \| SCENE= }}
Line 5:		Line 5:
	===Crystal Structure of the Y34F mutant of Saccharomyces cerevisiae Manganese Superoxide Dismutase===		===Crystal Structure of the Y34F mutant of Saccharomyces cerevisiae Manganese Superoxide Dismutase===

			{{ABSTRACT_PUBMED_22908245}}

	==About this Structure==		==About this Structure==

OCA at 06:05, 22 August 2012

2012-08-22T06:05:36Z

← Older revision		Revision as of 06:05, 22 August 2012
Line 1:		Line 1:
	~~'''Unreleased structure'''~~		[[Image:4e4e.jpg\|left\|200px]]

	~~The entry~~ 4e4e ~~is ON HOLD~~		{{STRUCTURE_4e4e\| PDB=4e4e \| SCENE= }}

	~~Authors: Sheng, Y., Cascio, D., Valentine, J.S.~~		===Crystal Structure of the Y34F mutant of Saccharomyces cerevisiae Manganese Superoxide Dismutase===

	~~Description~~: ~~Crystal Structure of the Y34F mutant of~~ Saccharomyces cerevisiae ~~Manganese~~ Superoxide ~~Dismutase~~
			==About this Structure==
			[[4e4e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E4E OCA].
			[[Category: Saccharomyces cerevisiae]]
			[[Category: Superoxide dismutase]]
			[[Category: Cascio, D.]]
			[[Category: Sheng, Y.]]
			[[Category: Valentine, J S.]]
			[[Category: Mn superoxide dismutase]]
			[[Category: Oxidoreductase]]

OCA at 07:21, 28 March 2012

2012-03-28T07:21:53Z

← Older revision		Revision as of 07:21, 28 March 2012
Line 3:		Line 3:
	The entry 4e4e is ON HOLD		The entry 4e4e is ON HOLD

	Authors: Sheng, Y, Cascio, D, Valentine, J.S.		Authors: Sheng, Y., Cascio, D., Valentine, J.S.

	Description: Crystal Structure of the Y34F mutant of Saccharomyces cerevisiae Manganese Superoxide Dismutase		Description: Crystal Structure of the Y34F mutant of Saccharomyces cerevisiae Manganese Superoxide Dismutase

OCA: Protected "4e4e" [edit=sysop:move=sysop]

2012-03-21T07:16:47Z

Protected "4e4e" [edit=sysop:move=sysop]

← Older revision	Revision as of 07:16, 21 March 2012
(No difference)

OCA: New page: '''Unreleased structure''' The entry 4e4e is ON HOLD Authors: Sheng, Y, Cascio, D, Valentine, J.S. Description: Crystal Structure of the Y34F mutant of Saccharomyces cerevisiae Mangane...

2012-03-21T07:16:46Z

New page: '''Unreleased structure''' The entry 4e4e is ON HOLD Authors: Sheng, Y, Cascio, D, Valentine, J.S. Description: Crystal Structure of the Y34F mutant of Saccharomyces cerevisiae Mangane...

New page

'''Unreleased structure'''

The entry 4e4e is ON HOLD

Authors: Sheng, Y, Cascio, D, Valentine, J.S.

Description: Crystal Structure of the Y34F mutant of Saccharomyces cerevisiae Manganese Superoxide Dismutase