4gdp - Revision history

OCA at 15:44, 14 March 2024

OCA — Thu, 14 Mar 2024 15:44:11 GMT

←Older revision		Revision as of 15:44, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4gdp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GDP FirstGlance]. <br>		<table><tr><td colspan='2'>[[4gdp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GDP FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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]] 1.9998Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=4gdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdp OCA], [https://pdbe.org/4gdp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gdp RCSB], [https://www.ebi.ac.uk/pdbsum/4gdp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gdp 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=4gdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdp OCA], [https://pdbe.org/4gdp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gdp RCSB], [https://www.ebi.ac.uk/pdbsum/4gdp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gdp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/FMS1_YEAST FMS1_YEAST] Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance.<ref>PMID:12670477</ref> <ref>PMID:14617780</ref>		[https://www.uniprot.org/uniprot/FMS1_YEAST FMS1_YEAST] Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance.<ref>PMID:12670477</ref> <ref>PMID:14617780</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Flavoprotein Fms1 from Saccharomyces cerevisiae catalyzes the oxidation of spermine in the biosynthetic pathway for pantothenic acid. The same reaction is catalyzed by the mammalian polyamine and spermine oxidases. The active site of Fms1 contains three amino acid residues positioned to interact with the polyamine substrate, His67, Asn195, and Asp94. These three residues form a hydrogen-bonding triad with Asn195 being the central residue. Previous studies of the effects of mutating His67 are consistent with that residue being important both for interacting with the substrate and for maintaining the hydrogen bonds in the triad [Adachi, M. S., Taylor, A. B., Hart, P. J., and Fitzpatrick, P. F. (2012) Biochemistry 51, 4888-4897]. The N195A and D94N enzymes have now been characterized to evaluate their roles in catalysis. Both mutations primarily affect the reductive half-reaction. With N(1)-acetylspermine as the substrate, the rate constant for flavin reduction decreases approximately 450-fold for both mutations; the effects with spermine as the substrate are smaller, 20-40-fold. The k(cat)/K(amine)- and k(cat)-pH profiles with N(1)-acetylspermine are only slightly changed from the profiles for the wild-type enzyme, consistent with the pK(a) values arising from the amine substrate or product and not from active site residues. The structure of the N195A enzyme was determined at a resolution of 2.0 A. The structure shows a molecule of tetraethylene glycol in the active site and establishes that the mutation has no effect on the protein structure. Overall, the results are consistent with the role of Asn195 and Asp94 being to properly position the polyamine substrate for oxidation.
-
-	Mechanistic and Structural Analyses of the Roles of Active Site Residues in Yeast Polyamine Oxidase Fms1: Characterization of the N195A and D94N Enzymes.,Adachi MS, Taylor AB, Hart PJ, Fitzpatrick PF Biochemistry. 2012 Oct 15. PMID:23034052<ref>PMID:23034052</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4gdp" style="background-color:#fffaf0;"></div>

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

OCA at 06:50, 26 October 2022

OCA — Wed, 26 Oct 2022 06:50:16 GMT

←Older revision		Revision as of 06:50, 26 October 2022
Line 1:		Line 1:

	==Yeast polyamine oxidase FMS1, N195A mutant==		==Yeast polyamine oxidase FMS1, N195A mutant==
-	<StructureSection load='4gdp' size='340' side='right' caption='[[4gdp]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='4gdp' size='340' side='right'caption='[[4gdp]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gdp]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Baker's_yeast Baker's yeast~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GDP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4GDP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gdp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GDP FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ech\|4ech]]</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=4gdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdp OCA], [https://pdbe.org/4gdp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gdp RCSB], [https://www.ebi.ac.uk/pdbsum/4gdp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gdp ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FMS1, YM9711.09, YMR020W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_polyamine_oxidase Non-specific polyamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.17 1.5.3.17] </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=4gdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdp OCA], [~~http~~://pdbe.org/4gdp PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4gdp RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4gdp PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4gdp ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FMS1_YEAST FMS1_YEAST]] Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance.<ref>PMID:12670477</ref> <ref>PMID:14617780</ref>	+	[https://www.uniprot.org/uniprot/FMS1_YEAST FMS1_YEAST] Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance.<ref>PMID:12670477</ref> <ref>PMID:14617780</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 28:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Baker's yeast~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Non-specific polyamine oxidase~~]]	+	[[Category: Saccharomyces cerevisiae S288C]]
-	[[Category: Adachi~~, M S~~]]	+	[[Category: Adachi MS]]
-	[[Category: Fitzpatrick~~, P F~~]]	+	[[Category: Fitzpatrick PF]]
-	[[Category: Hart~~, P J~~]]	+	[[Category: Hart PJ]]
-	[[Category: Taylor~~, A B]]~~	+	[[Category: Taylor AB]]
-	~~[[Category: Fad cofactor]]~~	+
-	~~[[Category: Flavoenzyme]]~~	+
-	~~[[Category: Mutant]]~~	+
-	~~[[Category: Oxidase]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 17:55, 5 August 2016

OCA — Fri, 05 Aug 2016 17:55:53 GMT

←Older revision		Revision as of 17:55, 5 August 2016
Line 1:		Line 1:
		+
	==Yeast polyamine oxidase FMS1, N195A mutant==		==Yeast polyamine oxidase FMS1, N195A mutant==
	<StructureSection load='4gdp' size='340' side='right' caption='[[4gdp]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4gdp' size='340' side='right' caption='[[4gdp]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gdp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GDP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GDP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gdp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GDP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GDP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ech\|4ech]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ech\|4ech]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FMS1, YM9711.09, YMR020W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 ~~Saccharomyces cerevisiae S288c~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FMS1, YM9711.09, YMR020W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_polyamine_oxidase Non-specific polyamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.17 1.5.3.17] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_polyamine_oxidase Non-specific polyamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.17 1.5.3.17] </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=4gdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gdp RCSB], [http://www.ebi.ac.uk/pdbsum/4gdp 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=4gdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdp OCA], [http://pdbe.org/4gdp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gdp RCSB], [http://www.ebi.ac.uk/pdbsum/4gdp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gdp 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 4gdp" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 26:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Baker's yeast]]
	[[Category: Non-specific polyamine oxidase]]		[[Category: Non-specific polyamine oxidase]]
-	[[Category: Saccharomyces cerevisiae s288c]]
	[[Category: Adachi, M S]]		[[Category: Adachi, M S]]
	[[Category: Fitzpatrick, P F]]		[[Category: Fitzpatrick, P F]]

OCA at 20:47, 25 December 2014

OCA — Thu, 25 Dec 2014 20:47:34 GMT

←Older revision		Revision as of 20:47, 25 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4gdp.~~png~~\|~~left~~\|~~200px~~]]	+	==Yeast polyamine oxidase FMS1, N195A mutant==
		+	<StructureSection load='4gdp' size='340' side='right' caption='[[4gdp]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4gdp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GDP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GDP FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ech\|4ech]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FMS1, YM9711.09, YMR020W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_polyamine_oxidase Non-specific polyamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.17 1.5.3.17] </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=4gdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gdp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gdp RCSB], [http://www.ebi.ac.uk/pdbsum/4gdp PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FMS1_YEAST FMS1_YEAST]] Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance.<ref>PMID:12670477</ref> <ref>PMID:14617780</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Flavoprotein Fms1 from Saccharomyces cerevisiae catalyzes the oxidation of spermine in the biosynthetic pathway for pantothenic acid. The same reaction is catalyzed by the mammalian polyamine and spermine oxidases. The active site of Fms1 contains three amino acid residues positioned to interact with the polyamine substrate, His67, Asn195, and Asp94. These three residues form a hydrogen-bonding triad with Asn195 being the central residue. Previous studies of the effects of mutating His67 are consistent with that residue being important both for interacting with the substrate and for maintaining the hydrogen bonds in the triad [Adachi, M. S., Taylor, A. B., Hart, P. J., and Fitzpatrick, P. F. (2012) Biochemistry 51, 4888-4897]. The N195A and D94N enzymes have now been characterized to evaluate their roles in catalysis. Both mutations primarily affect the reductive half-reaction. With N(1)-acetylspermine as the substrate, the rate constant for flavin reduction decreases approximately 450-fold for both mutations; the effects with spermine as the substrate are smaller, 20-40-fold. The k(cat)/K(amine)- and k(cat)-pH profiles with N(1)-acetylspermine are only slightly changed from the profiles for the wild-type enzyme, consistent with the pK(a) values arising from the amine substrate or product and not from active site residues. The structure of the N195A enzyme was determined at a resolution of 2.0 A. The structure shows a molecule of tetraethylene glycol in the active site and establishes that the mutation has no effect on the protein structure. Overall, the results are consistent with the role of Asn195 and Asp94 being to properly position the polyamine substrate for oxidation.

-	~~{{STRUCTURE_4gdp\| PDB=4gdp \| SCENE= }}~~	+	Mechanistic and Structural Analyses of the Roles of Active Site Residues in Yeast Polyamine Oxidase Fms1: Characterization of the N195A and D94N Enzymes.,Adachi MS, Taylor AB, Hart PJ, Fitzpatrick PF Biochemistry. 2012 Oct 15. PMID:23034052<ref>PMID:23034052</ref>

-	~~===Yeast polyamine oxidase FMS1~~, ~~N195A mutant===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_23034052}}~~	+	==See Also==
-		+	*[[Polyamine oxidase\|Polyamine oxidase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~4gdp~~]] ~~is a 4 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GDP OCA].~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Non-specific polyamine oxidase]]		[[Category: Non-specific polyamine oxidase]]
	[[Category: Saccharomyces cerevisiae s288c]]		[[Category: Saccharomyces cerevisiae s288c]]
-	[[Category: Adachi, M S.]]	+	[[Category: Adachi, M S]]
-	[[Category: Fitzpatrick, P F.]]	+	[[Category: Fitzpatrick, P F]]
-	[[Category: Hart, P J.]]	+	[[Category: Hart, P J]]
-	[[Category: Taylor, A B.]]	+	[[Category: Taylor, A B]]
	[[Category: Fad cofactor]]		[[Category: Fad cofactor]]
	[[Category: Flavoenzyme]]		[[Category: Flavoenzyme]]

OCA at 12:50, 30 January 2013

OCA — Wed, 30 Jan 2013 12:50:59 GMT

←Older revision		Revision as of 12:50, 30 January 2013
Line 1:		Line 1:
-	[[Image:4gdp.~~jpg~~\|left\|200px]]	+	[[Image:4gdp.png\|left\|200px]]

	{{STRUCTURE_4gdp\| PDB=4gdp \| SCENE= }}		{{STRUCTURE_4gdp\| PDB=4gdp \| SCENE= }}

OCA at 07:01, 17 October 2012

OCA — Wed, 17 Oct 2012 07:01:47 GMT

←Older revision		Revision as of 07:01, 17 October 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4gdp.jpg\|left\|200px]]

-	~~The entry~~ 4gdp ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4gdp\| PDB=4gdp \| SCENE= }}

-	~~Authors: Taylor~~, ~~A.B., Adachi, M.S., Hart, P.J., Fitzpatrick, P.F.~~	+	===Yeast polyamine oxidase FMS1, N195A mutant===

-	~~Description~~: ~~Yeast~~ polyamine oxidase ~~FMS1~~, ~~N195A mutant~~	+	{{ABSTRACT_PUBMED_23034052}}
		+
		+	==About this Structure==
		+	[[4gdp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GDP OCA].
		+	[[Category: Non-specific polyamine oxidase]]
		+	[[Category: Saccharomyces cerevisiae s288c]]
		+	[[Category: Adachi, M S.]]
		+	[[Category: Fitzpatrick, P F.]]
		+	[[Category: Hart, P J.]]
		+	[[Category: Taylor, A B.]]
		+	[[Category: Fad cofactor]]
		+	[[Category: Flavoenzyme]]
		+	[[Category: Mutant]]
		+	[[Category: Oxidase]]
		+	[[Category: Oxidoreductase]]

OCA at 04:50, 12 September 2012

OCA — Wed, 12 Sep 2012 04:50:19 GMT

←Older revision		Revision as of 04:50, 12 September 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4gdp is ON HOLD	+	The entry 4gdp is ON HOLD until Paper Publication

	Authors: Taylor, A.B., Adachi, M.S., Hart, P.J., Fitzpatrick, P.F.		Authors: Taylor, A.B., Adachi, M.S., Hart, P.J., Fitzpatrick, P.F.

	Description: Yeast polyamine oxidase FMS1, N195A mutant		Description: Yeast polyamine oxidase FMS1, N195A mutant

OCA at 05:33, 22 August 2012

OCA — Wed, 22 Aug 2012 05:33:27 GMT

←Older revision		Revision as of 05:33, 22 August 2012
Line 5:		Line 5:
	Authors: Taylor, A.B., Adachi, M.S., Hart, P.J., Fitzpatrick, P.F.		Authors: Taylor, A.B., Adachi, M.S., Hart, P.J., Fitzpatrick, P.F.

-	Description: ~~YEAST POLYAMINE OXIDASE~~ FMS1, N195A ~~MUTANT~~	+	Description: Yeast polyamine oxidase FMS1, N195A mutant

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

OCA — Wed, 08 Aug 2012 05:01:36 GMT

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

←Older revision

Revision as of 05:01, 8 August 2012

OCA: New page: '''Unreleased structure''' The entry 4gdp is ON HOLD Authors: Taylor, A.B., Adachi, M.S., Hart, P.J., Fitzpatrick, P.F. Description: YEAST POLYAMINE OXIDASE FMS1, N195A MUTANT

OCA — Wed, 08 Aug 2012 05:01:35 GMT

New page: '''Unreleased structure''' The entry 4gdp is ON HOLD Authors: Taylor, A.B., Adachi, M.S., Hart, P.J., Fitzpatrick, P.F. Description: YEAST POLYAMINE OXIDASE FMS1, N195A MUTANT

New page

'''Unreleased structure'''

The entry 4gdp is ON HOLD

Authors: Taylor, A.B., Adachi, M.S., Hart, P.J., Fitzpatrick, P.F.

Description: YEAST POLYAMINE OXIDASE FMS1, N195A MUTANT