4fag - Revision history

OCA at 11:13, 1 March 2024

2024-03-01T11:13:18Z

←Older revision		Revision as of 11:13, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fag]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudaminobacter_salicylatoxidans Pseudaminobacter salicylatoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FAG FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fag]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudaminobacter_salicylatoxidans Pseudaminobacter salicylatoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FAG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTQ:2,5-DIHYDROXYBENZOIC+ACID'>GTQ</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]] 2.5Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTQ:2,5-DIHYDROXYBENZOIC+ACID'>GTQ</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=4fag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fag OCA], [https://pdbe.org/4fag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fag RCSB], [https://www.ebi.ac.uk/pdbsum/4fag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fag 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=4fag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fag OCA], [https://pdbe.org/4fag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fag RCSB], [https://www.ebi.ac.uk/pdbsum/4fag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fag ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/Q67FT0_PSESE Q67FT0_PSESE]		[https://www.uniprot.org/uniprot/Q67FT0_PSESE Q67FT0_PSESE]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Key amino acid residues of the salicylate 1,2-dioxygenase (SDO), an iron (II) class III ring cleaving dioxygenase from Pseudaminobacter salicylatoxidans BN12, were selected, based on amino acid sequence alignments and structural analysis of the enzyme, and modified by site-directed mutagenesis to obtain variant forms with altered catalytic properties. SDO shares with 1-hydroxy-2-naphthoate dioxygenase (1H2NDO) its unique ability to oxidatively cleave monohydroxylated aromatic compounds. Nevertheless SDO is more versatile with respect to 1H2NDO and other known gentisate dioxygenases (GDOs) because it cleaves not only gentisate and 1-hydroxy-2-naphthoate (1H2NC) but also salicylate and substituted salicylates. Several enzyme variants of SDO were rationally designed to simulate 1H2NDO. The basic kinetic parameters for the SDO mutants L38Q, M46V, A85H and W104Y were determined. The enzyme variants L38Q, M46V, A85H demonstrated higher catalytic efficiencies toward 1-hydroxy-2-naphthoate (1H2NC) compared to gentisate. Remarkably, the enzyme variant A85H effectively cleaved 1H2NC but did not oxidize gentisate at all. The W104Y SDO mutant exhibited reduced reaction rates for all substrates tested. The crystal structures of the A85H and W104Y variants were solved and analyzed. The substitution of Ala85 with a histidine residue caused significant changes in the orientation of the loop containing this residue which is involved in the active site closing upon substrate binding. In SDO A85H this specific loop shifts away from the active site and thus opens the cavity favoring the binding of bulkier substrates. Since this loop also interacts with the N-terminal residues of the vicinal subunit, the structure and packing of the holoenzyme might be also affected.
-
-	The generation of a 1-hydroxy-2-naphthoate 1,2-dioxygenase by single point mutations of salicylate 1,2-dioxygenase - Rational design of mutants and the crystal structures of the A85H and W104Y variants.,Ferraroni M, Steimer L, Matera I, Burger S, Scozzafava A, Stolz A, Briganti F J Struct Biol. 2012 Aug 31. pii: S1047-8477(12)00238-9. doi:, 10.1016/j.jsb.2012.08.007. PMID:22960182<ref>PMID:22960182</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4fag" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Dioxygenase 3D structures\|Dioxygenase 3D structures]]		*[[Dioxygenase 3D structures\|Dioxygenase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 04:45, 7 October 2022

2022-10-07T04:45:02Z

←Older revision		Revision as of 04:45, 7 October 2022
Line 3:		Line 3:
	<StructureSection load='4fag' size='340' side='right'caption='[[4fag]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='4fag' size='340' side='right'caption='[[4fag]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4fag]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Cip_106963 Cip 106963~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FAG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4FAG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4fag]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudaminobacter_salicylatoxidans Pseudaminobacter salicylatoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FAG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTQ:2,5-DIHYDROXYBENZOIC+ACID'>GTQ</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTQ:2,5-DIHYDROXYBENZOIC+ACID'>GTQ</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fah\|4fah]], [[4fbf\|4fbf]]</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=4fag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fag OCA], [https://pdbe.org/4fag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fag RCSB], [https://www.ebi.ac.uk/pdbsum/4fag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fag ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Gentisate_1,2-dioxygenase Gentisate 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.4 1.13.11.4] </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=4fag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fag OCA], [~~http~~://pdbe.org/4fag PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4fag RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4fag PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4fag ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/Q67FT0_PSESE Q67FT0_PSESE]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 20:

	==See Also==		==See Also==
-	*[[Dioxygenase\|Dioxygenase]]	+	*[[Dioxygenase 3D structures\|Dioxygenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Cip 106963]]
-	[[Category: Gentisate 1,2-dioxygenase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Briganti, F~~]]	+	[[Category: Pseudaminobacter salicylatoxidans]]
-	[[Category: ~~Ferraroni, M~~]]	+	[[Category: Briganti F]]
-	[[Category: ~~Matera, I~~]]	+	[[Category: Ferraroni M]]
-	[[Category: ~~Aromatic compound degradation]]~~	+	[[Category: Matera I]]
-	~~[[Category: Beta-sandwich]]~~	+
-	~~[[Category: Dioxygenase]]~~	+
-	~~[[Category: Metalloprotein]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 07:51, 27 March 2019

2019-03-27T07:51:40Z

←Older revision		Revision as of 07:51, 27 March 2019
Line 1:		Line 1:

	==Crystal Structure of the Salicylate 1,2-dioxygenase from Pseudoaminobacter salicylatoxidans W104Y mutant in complex with gentisate==		==Crystal Structure of the Salicylate 1,2-dioxygenase from Pseudoaminobacter salicylatoxidans W104Y mutant in complex with gentisate==
-	<StructureSection load='4fag' size='340' side='right' caption='[[4fag]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='4fag' size='340' side='right'caption='[[4fag]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fag]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cip_106963 Cip 106963]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FAG FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fag]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cip_106963 Cip 106963]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FAG FirstGlance]. <br>
Line 27:		Line 27:
	[[Category: Cip 106963]]		[[Category: Cip 106963]]
	[[Category: Gentisate 1,2-dioxygenase]]		[[Category: Gentisate 1,2-dioxygenase]]
		+	[[Category: Large Structures]]
	[[Category: Briganti, F]]		[[Category: Briganti, F]]
	[[Category: Ferraroni, M]]		[[Category: Ferraroni, M]]

OCA at 19:48, 15 December 2016

2016-12-15T19:48:34Z

←Older revision		Revision as of 19:48, 15 December 2016
Line 1:		Line 1:
		+
	==Crystal Structure of the Salicylate 1,2-dioxygenase from Pseudoaminobacter salicylatoxidans W104Y mutant in complex with gentisate==		==Crystal Structure of the Salicylate 1,2-dioxygenase from Pseudoaminobacter salicylatoxidans W104Y mutant in complex with gentisate==
	<StructureSection load='4fag' size='340' side='right' caption='[[4fag]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='4fag' size='340' side='right' caption='[[4fag]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4fag]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Pseudaminobacter_salicylatoxidans Pseudaminobacter salicylatoxidans~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FAG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4fag]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cip_106963 Cip 106963]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FAG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTQ:2,5-DIHYDROXYBENZOIC+ACID'>GTQ</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTQ:2,5-DIHYDROXYBENZOIC+ACID'>GTQ</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fah\|4fah]], [[4fbf\|4fbf]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fah\|4fah]], [[4fbf\|4fbf]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Gentisate_1,2-dioxygenase Gentisate 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.4 1.13.11.4] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Gentisate_1,2-dioxygenase Gentisate 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.4 1.13.11.4] </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=4fag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fag OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fag RCSB], [http://www.ebi.ac.uk/pdbsum/4fag 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=4fag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fag OCA], [http://pdbe.org/4fag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fag RCSB], [http://www.ebi.ac.uk/pdbsum/4fag PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fag 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 4fag" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 23:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Cip 106963]]
	[[Category: Gentisate 1,2-dioxygenase]]		[[Category: Gentisate 1,2-dioxygenase]]
-	[[Category: Pseudaminobacter salicylatoxidans]]
	[[Category: Briganti, F]]		[[Category: Briganti, F]]
	[[Category: Ferraroni, M]]		[[Category: Ferraroni, M]]

OCA at 15:29, 9 December 2014

2014-12-09T15:29:00Z

←Older revision		Revision as of 15:29, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4fag.~~png~~\|~~left~~\|~~200px~~]]	+	==Crystal Structure of the Salicylate 1,2-dioxygenase from Pseudoaminobacter salicylatoxidans W104Y mutant in complex with gentisate==
		+	<StructureSection load='4fag' size='340' side='right' caption='[[4fag]], [[Resolution\|resolution]] 2.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4fag]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudaminobacter_salicylatoxidans Pseudaminobacter salicylatoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FAG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FAG FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTQ:2,5-DIHYDROXYBENZOIC+ACID'>GTQ</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fah\|4fah]], [[4fbf\|4fbf]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Gentisate_1,2-dioxygenase Gentisate 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.4 1.13.11.4] </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=4fag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fag OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fag RCSB], [http://www.ebi.ac.uk/pdbsum/4fag PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Key amino acid residues of the salicylate 1,2-dioxygenase (SDO), an iron (II) class III ring cleaving dioxygenase from Pseudaminobacter salicylatoxidans BN12, were selected, based on amino acid sequence alignments and structural analysis of the enzyme, and modified by site-directed mutagenesis to obtain variant forms with altered catalytic properties. SDO shares with 1-hydroxy-2-naphthoate dioxygenase (1H2NDO) its unique ability to oxidatively cleave monohydroxylated aromatic compounds. Nevertheless SDO is more versatile with respect to 1H2NDO and other known gentisate dioxygenases (GDOs) because it cleaves not only gentisate and 1-hydroxy-2-naphthoate (1H2NC) but also salicylate and substituted salicylates. Several enzyme variants of SDO were rationally designed to simulate 1H2NDO. The basic kinetic parameters for the SDO mutants L38Q, M46V, A85H and W104Y were determined. The enzyme variants L38Q, M46V, A85H demonstrated higher catalytic efficiencies toward 1-hydroxy-2-naphthoate (1H2NC) compared to gentisate. Remarkably, the enzyme variant A85H effectively cleaved 1H2NC but did not oxidize gentisate at all. The W104Y SDO mutant exhibited reduced reaction rates for all substrates tested. The crystal structures of the A85H and W104Y variants were solved and analyzed. The substitution of Ala85 with a histidine residue caused significant changes in the orientation of the loop containing this residue which is involved in the active site closing upon substrate binding. In SDO A85H this specific loop shifts away from the active site and thus opens the cavity favoring the binding of bulkier substrates. Since this loop also interacts with the N-terminal residues of the vicinal subunit, the structure and packing of the holoenzyme might be also affected.

-	~~{{STRUCTURE_4fag\| PDB=4fag \| SCENE= }}~~	+	The generation of a 1-hydroxy-2-naphthoate 1,2-dioxygenase by single point mutations of salicylate 1,2-dioxygenase - Rational design of mutants and the crystal structures of the A85H and W104Y variants.,Ferraroni M, Steimer L, Matera I, Burger S, Scozzafava A, Stolz A, Briganti F J Struct Biol. 2012 Aug 31. pii: S1047-8477(12)00238-9. doi:, 10.1016/j.jsb.2012.08.007. PMID:22960182<ref>PMID:22960182</ref>

-	~~===Crystal Structure~~ of the ~~Salicylate 1,2-dioxygenase from Pseudoaminobacter salicylatoxidans W104Y mutant in complex with gentisate===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_22960182}}~~	+	==See Also==
-		+	*[[Dioxygenase\|Dioxygenase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~4fag~~]] ~~is a 1 chain structure with sequence from [http:~~//en.wikipedia.org/wiki/Pseudaminobacter_salicylatoxidans Pseudaminobacter salicylatoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FAG OCA].	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Gentisate 1,2-dioxygenase]]		[[Category: Gentisate 1,2-dioxygenase]]
	[[Category: Pseudaminobacter salicylatoxidans]]		[[Category: Pseudaminobacter salicylatoxidans]]
-	[[Category: Briganti, F.]]	+	[[Category: Briganti, F]]
-	[[Category: Ferraroni, M.]]	+	[[Category: Ferraroni, M]]
-	[[Category: Matera, I.]]	+	[[Category: Matera, I]]
	[[Category: Aromatic compound degradation]]		[[Category: Aromatic compound degradation]]
	[[Category: Beta-sandwich]]		[[Category: Beta-sandwich]]

OCA at 14:45, 28 November 2012

2012-11-28T14:45:13Z

←Older revision		Revision as of 14:45, 28 November 2012
Line 1:		Line 1:
-	[[Image:4fag.~~jpg~~\|left\|200px]]	+	[[Image:4fag.png\|left\|200px]]

	{{STRUCTURE_4fag\| PDB=4fag \| SCENE= }}		{{STRUCTURE_4fag\| PDB=4fag \| SCENE= }}

OCA at 20:29, 26 September 2012

2012-09-26T20:29:44Z

←Older revision		Revision as of 20:29, 26 September 2012
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-	~~'''Unreleased structure'''~~	+	[[Image:4fag.jpg\|left\|200px]]

-	~~The entry~~ 4fag ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4fag\| PDB=4fag \| SCENE= }}

-	~~Authors: Ferraroni~~, ~~M., Briganti, F., Matera, I.~~	+	===Crystal Structure of the Salicylate 1,2-dioxygenase from Pseudoaminobacter salicylatoxidans W104Y mutant in complex with gentisate===

-	~~Description: Crystal~~ Structure ~~of the Salicylate~~ 1,2-dioxygenase ~~from Pseudoaminobacter~~ salicylatoxidans ~~W104Y mutant in complex with gentisate~~	+	{{ABSTRACT_PUBMED_22960182}}
		+
		+	==About this Structure==
		+	[[4fag]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudaminobacter_salicylatoxidans Pseudaminobacter salicylatoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FAG OCA].
		+	[[Category: Gentisate 1,2-dioxygenase]]
		+	[[Category: Pseudaminobacter salicylatoxidans]]
		+	[[Category: Briganti, F.]]
		+	[[Category: Ferraroni, M.]]
		+	[[Category: Matera, I.]]
		+	[[Category: Aromatic compound degradation]]
		+	[[Category: Beta-sandwich]]
		+	[[Category: Dioxygenase]]
		+	[[Category: Metalloprotein]]
		+	[[Category: Oxidoreductase]]

OCA at 05:48, 13 June 2012

2012-06-13T05:48:56Z

←Older revision		Revision as of 05:48, 13 June 2012
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	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Ferraroni, M., Briganti, F., Matera, I.		Authors: Ferraroni, M., Briganti, F., Matera, I.

	Description: Crystal Structure of the Salicylate 1,2-dioxygenase from Pseudoaminobacter salicylatoxidans W104Y mutant in complex with gentisate		Description: Crystal Structure of the Salicylate 1,2-dioxygenase from Pseudoaminobacter salicylatoxidans W104Y mutant in complex with gentisate

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

2012-05-30T05:33:45Z

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

←Older revision

Revision as of 05:33, 30 May 2012

OCA: New page: '''Unreleased structure''' The entry 4fag is ON HOLD Authors: Ferraroni, M., Briganti, F., Matera, I. Description: Crystal Structure of the Salicylate 1,2-dioxygenase from Pseudoaminob...

2012-05-30T05:33:45Z

New page: '''Unreleased structure''' The entry 4fag is ON HOLD Authors: Ferraroni, M., Briganti, F., Matera, I. Description: Crystal Structure of the Salicylate 1,2-dioxygenase from Pseudoaminob...

New page

'''Unreleased structure'''

The entry 4fag is ON HOLD

Authors: Ferraroni, M., Briganti, F., Matera, I.

Description: Crystal Structure of the Salicylate 1,2-dioxygenase from Pseudoaminobacter salicylatoxidans W104Y mutant in complex with gentisate