4c5o - Revision history

OCA at 12:04, 20 December 2023

OCA — Wed, 20 Dec 2023 12:04:23 GMT

←Older revision		Revision as of 12:04, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c5o]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia Stenotrophomonas maltophilia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C5O FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c5o]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia Stenotrophomonas maltophilia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C5O 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=SO4:SULFATE+ION'>SO4</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]] 2.6Å</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=SO4:SULFATE+ION'>SO4</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=4c5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5o OCA], [https://pdbe.org/4c5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c5o RCSB], [https://www.ebi.ac.uk/pdbsum/4c5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5o 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=4c5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5o OCA], [https://pdbe.org/4c5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c5o RCSB], [https://www.ebi.ac.uk/pdbsum/4c5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5o ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/B2FRL2_STRMK B2FRL2_STRMK]]	+	[https://www.uniprot.org/uniprot/B2FRL2_STRMK B2FRL2_STRMK]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The flavoprotein monooxygenase (FPMO) from Stenotrophomonas maltophilia (SMFMO, Uniprot: B2FLR2) catalyses the asymmetric oxidation of thioethers and is unusual amongst FPMOs in its ability to use the non-phosphorylated cofactor NADH, as well as NADPH, for the reduction of the FAD coenzyme. In order to explore the basis for cofactor promiscuity, structure-guided mutation of two residues in the cofactor binding site, Gln193 and His194, in SMFMO were performed in an attempt to imitate the cofactor binding site of the NADPH-dependent FMO from Methylophaga aminisulfidivorans sp. SK1 (mFMO), in which structurally homologous residues Arg234 and Thr235 bind the NADPH 2'-ribose phosphate. Mutation of His194 to threonine proved most significant, with a switch in specificity from NADH to NADPH [(k cat/K m NADH)/k cat/K m NADPH) from 1.5:1 to 1:3.5, mostly as a result of a reduced K m for NADPH of approximately sevenfold in the His194Thr mutant. The structure of the Gln193Arg/His194Thr mutant revealed no substantial changes in the backbone of the enzyme or orientation of side chains resulting from mutation. Mutation of Phe52, in the vicinity of FAD, and which in mFMO is an asparagine thought to be responsible for flavin hydroperoxide stabilisation, is, in SMFMO, a determinant of enantioselectivity in sulfoxidation. Mutation of Phe52 to valine resulted in a mutant that transformed para-tolyl methyl sulfide into the (S)-sulfoxide with 32% e.e., compared to 25% (R)- for the wild type. These results shed further light both on the cofactor specificity of FPMOs, and their determinants of enantioselectivity, with a view to informing engineering studies of FPMOs in the future.
		+
		+	Mutations of an NAD(P)H-dependent flavoprotein monooxygenase that influence cofactor promiscuity and enantioselectivity.,Jensen CN, Ali ST, Allen MJ, Grogan G FEBS Open Bio. 2013 Sep 29;3:473-8. doi: 10.1016/j.fob.2013.09.008. eCollection, 2013. PMID:24251114<ref>PMID:24251114</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4c5o" style="background-color:#fffaf0;"></div>

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

OCA at 17:28, 7 September 2022

OCA — Wed, 07 Sep 2022 17:28:13 GMT

←Older revision		Revision as of 17:28, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4c5o' size='340' side='right'caption='[[4c5o]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='4c5o' size='340' side='right'caption='[[4c5o]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c5o]] is a 8 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"pseudomonas_maltophilia"_hugh_and_ryschenkow_1961 "pseudomonas~~ maltophilia~~" hugh and ryschenkow 1961~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5O OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4C5O FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c5o]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia Stenotrophomonas maltophilia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C5O 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=SO4:SULFATE+ION'>SO4</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=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Flavin-containing_monooxygenase Flavin-containing monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.8 1.14.13.8] </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=4c5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5o OCA], [https://pdbe.org/4c5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c5o RCSB], [https://www.ebi.ac.uk/pdbsum/4c5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5o ProSAT]</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=4c5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5o OCA], [~~http~~://pdbe.org/4c5o PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4c5o RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4c5o PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5o ProSAT]</span></td></tr>	+
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[[https://www.uniprot.org/uniprot/B2FRL2_STRMK B2FRL2_STRMK]]
-	The flavoprotein monooxygenase (FPMO) from Stenotrophomonas maltophilia (SMFMO, Uniprot: B2FLR2) catalyses the asymmetric oxidation of thioethers and is unusual amongst FPMOs in its ability to use the non-phosphorylated cofactor NADH, as well as NADPH, for the reduction of the FAD coenzyme. In order to explore the basis for cofactor promiscuity, structure-guided mutation of two residues in the cofactor binding site, Gln193 and His194, in SMFMO were performed in an attempt to imitate the cofactor binding site of the NADPH-dependent FMO from Methylophaga aminisulfidivorans sp. SK1 (mFMO), in which structurally homologous residues Arg234 and Thr235 bind the NADPH 2'-ribose phosphate. Mutation of His194 to threonine proved most significant, with a switch in specificity from NADH to NADPH [~~(k cat/K m NADH)/k cat/K m NADPH) from 1.5~~:~~1 to 1:3.5, mostly as a result of a reduced K m for NADPH of approximately sevenfold in the His194Thr mutant. The structure of the Gln193Arg~~/His194Thr mutant revealed no substantial changes in the backbone of the enzyme or orientation of side chains resulting from mutation. Mutation of Phe52, in the vicinity of FAD, and which in mFMO is an asparagine thought to be responsible for flavin hydroperoxide stabilisation, is, in SMFMO, a determinant of enantioselectivity in sulfoxidation. Mutation of Phe52 to valine resulted in a mutant that transformed para-tolyl methyl sulfide into the (S)-sulfoxide with 32% e.e., compared to 25% (R)- for the wild type. These results shed further light both on the cofactor specificity of FPMOs, and their determinants of enantioselectivity, with a view to informing engineering studies of FPMOs in the future.	+
-		+
-	Mutations of an NAD(P)H-dependent flavoprotein monooxygenase that influence cofactor promiscuity and enantioselectivity.,Jensen CN, Ali ST, Allen MJ, Grogan G FEBS Open Bio. 2013 Sep 29;3:473-8. doi: 10.1016/j.~~fob~~.~~2013.09.008. eCollection, 2013. PMID:24251114<ref>PMID:24251114<~~/~~ref>~~	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4c5o" style="background-color:#fffaf0;"><~~/~~div>~~	+

	==See Also==		==See Also==
-	*[[Monooxygenase\|Monooxygenase]]	+	*[[Monooxygenase 3D structures\|Monooxygenase 3D structures]]
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Pseudomonas maltophilia hugh and ryschenkow 1961]]
-	[[Category: Flavin-containing monooxygenase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Ali, S T~~]]	+	[[Category: Stenotrophomonas maltophilia]]
-	[[Category: ~~Allen, M J~~]]	+	[[Category: Ali ST]]
-	[[Category: ~~Grogan, G~~]]	+	[[Category: Allen MJ]]
-	[[Category: ~~Jensen, C N~~]]	+	[[Category: Grogan G]]
-	[[Category: ~~Oxidoreductase~~]]	+	[[Category: Jensen CN]]

OCA at 09:54, 20 March 2019

OCA — Wed, 20 Mar 2019 09:54:59 GMT

←Older revision		Revision as of 09:54, 20 March 2019
Line 1:		Line 1:

	==Flavin monooxygenase from Stenotrophomonas maltophilia. Q193R H194T mutant==		==Flavin monooxygenase from Stenotrophomonas maltophilia. Q193R H194T mutant==
-	<StructureSection load='4c5o' size='340' side='right' caption='[[4c5o]], [[Resolution\|resolution]] 2.60Å' scene=''>	+	<StructureSection load='4c5o' size='340' side='right'caption='[[4c5o]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c5o]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"pseudomonas_maltophilia"_hugh_and_ryschenkow_1961 "pseudomonas maltophilia" hugh and ryschenkow 1961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C5O FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c5o]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"pseudomonas_maltophilia"_hugh_and_ryschenkow_1961 "pseudomonas maltophilia" hugh and ryschenkow 1961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C5O FirstGlance]. <br>
Line 17:		Line 17:
	</div>		</div>
	<div class="pdbe-citations 4c5o" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4c5o" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Monooxygenase\|Monooxygenase]]
	== References ==		== References ==
	<references/>		<references/>
Line 23:		Line 26:
	[[Category: Pseudomonas maltophilia hugh and ryschenkow 1961]]		[[Category: Pseudomonas maltophilia hugh and ryschenkow 1961]]
	[[Category: Flavin-containing monooxygenase]]		[[Category: Flavin-containing monooxygenase]]
		+	[[Category: Large Structures]]
	[[Category: Ali, S T]]		[[Category: Ali, S T]]
	[[Category: Allen, M J]]		[[Category: Allen, M J]]

OCA at 14:56, 11 August 2016

OCA — Thu, 11 Aug 2016 14:56:09 GMT

←Older revision		Revision as of 14:56, 11 August 2016
Line 1:		Line 1:
		+
	==Flavin monooxygenase from Stenotrophomonas maltophilia. Q193R H194T mutant==		==Flavin monooxygenase from Stenotrophomonas maltophilia. Q193R H194T mutant==
	<StructureSection load='4c5o' size='340' side='right' caption='[[4c5o]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='4c5o' size='340' side='right' caption='[[4c5o]], [[Resolution\|resolution]] 2.60Å' scene=''>
Line 5:		Line 6:
	</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=SO4:SULFATE+ION'>SO4</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=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Flavin-containing_monooxygenase Flavin-containing monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.8 1.14.13.8] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Flavin-containing_monooxygenase Flavin-containing monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.8 1.14.13.8] </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=4c5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c5o RCSB], [http://www.ebi.ac.uk/pdbsum/4c5o 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=4c5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5o OCA], [http://pdbe.org/4c5o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c5o RCSB], [http://www.ebi.ac.uk/pdbsum/4c5o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5o ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 15:		Line 16:
	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 4c5o" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:24, 4 January 2015

OCA — Sun, 04 Jan 2015 13:24:50 GMT

←Older revision		Revision as of 13:24, 4 January 2015
Line 1:		Line 1:
-	~~{{STRUCTURE_4c5o~~\| ~~PDB~~=4c5o \| ~~SCENE~~= }}	+	==Flavin monooxygenase from Stenotrophomonas maltophilia. Q193R H194T mutant==
-	===Flavin monooxygenase ~~from Stenotrophomonas maltophilia~~. ~~Q193R H194T mutant~~===	+	<StructureSection load='4c5o' size='340' side='right' caption='[[4c5o]], [[Resolution\|resolution]] 2.60Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24251114}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4c5o]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"pseudomonas_maltophilia"_hugh_and_ryschenkow_1961 "pseudomonas maltophilia" hugh and ryschenkow 1961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C5O 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=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Flavin-containing_monooxygenase Flavin-containing monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.8 1.14.13.8] </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=4c5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c5o RCSB], [http://www.ebi.ac.uk/pdbsum/4c5o PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The flavoprotein monooxygenase (FPMO) from Stenotrophomonas maltophilia (SMFMO, Uniprot: B2FLR2) catalyses the asymmetric oxidation of thioethers and is unusual amongst FPMOs in its ability to use the non-phosphorylated cofactor NADH, as well as NADPH, for the reduction of the FAD coenzyme. In order to explore the basis for cofactor promiscuity, structure-guided mutation of two residues in the cofactor binding site, Gln193 and His194, in SMFMO were performed in an attempt to imitate the cofactor binding site of the NADPH-dependent FMO from Methylophaga aminisulfidivorans sp. SK1 (mFMO), in which structurally homologous residues Arg234 and Thr235 bind the NADPH 2'-ribose phosphate. Mutation of His194 to threonine proved most significant, with a switch in specificity from NADH to NADPH [(k cat/K m NADH)/k cat/K m NADPH) from 1.5:1 to 1:3.5, mostly as a result of a reduced K m for NADPH of approximately sevenfold in the His194Thr mutant. The structure of the Gln193Arg/His194Thr mutant revealed no substantial changes in the backbone of the enzyme or orientation of side chains resulting from mutation. Mutation of Phe52, in the vicinity of FAD, and which in mFMO is an asparagine thought to be responsible for flavin hydroperoxide stabilisation, is, in SMFMO, a determinant of enantioselectivity in sulfoxidation. Mutation of Phe52 to valine resulted in a mutant that transformed para-tolyl methyl sulfide into the (S)-sulfoxide with 32% e.e., compared to 25% (R)- for the wild type. These results shed further light both on the cofactor specificity of FPMOs, and their determinants of enantioselectivity, with a view to informing engineering studies of FPMOs in the future.

-	~~==About this Structure==~~	+	Mutations of an NAD(P)H-dependent flavoprotein monooxygenase that influence cofactor promiscuity and enantioselectivity.,Jensen CN, Ali ST, Allen MJ, Grogan G FEBS Open Bio. 2013 Sep 29;3:473-8. doi: 10.1016/j.fob.2013.09.008. eCollection, 2013. PMID:24251114<ref>PMID:24251114</ref>
-	~~[[4c5o]] is a~~ 8 ~~chain structure~~. ~~Full crystallographic information is available from [http~~:/~~/oca~~.~~weizmann~~.ac.~~il/oca-bin/ocashort?id=4C5O OCA]~~.	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024251114</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Pseudomonas maltophilia hugh and ryschenkow 1961]]
	[[Category: Flavin-containing monooxygenase]]		[[Category: Flavin-containing monooxygenase]]
-	[[Category: Ali, S T.]]	+	[[Category: Ali, S T]]
-	[[Category: Allen, M J.]]	+	[[Category: Allen, M J]]
-	[[Category: Grogan, G.]]	+	[[Category: Grogan, G]]
-	[[Category: Jensen, C N.]]	+	[[Category: Jensen, C N]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 17:31, 19 February 2014

OCA — Wed, 19 Feb 2014 17:31:41 GMT

←Older revision		Revision as of 17:31, 19 February 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4c5o\| PDB=4c5o \| SCENE= }}
		+	===Flavin monooxygenase from Stenotrophomonas maltophilia. Q193R H194T mutant===
		+	{{ABSTRACT_PUBMED_24251114}}

-	~~The entry~~ 4c5o is ~~ON HOLD~~	+	==About this Structure==
		+	[[4c5o]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5O OCA].

-	~~Authors~~: ~~Jensen, C.N.,~~ Ali, S.T., Allen, M.J., Grogan, G.	+	==Reference==
-		+	<ref group="xtra">PMID:024251114</ref><references group="xtra"/><references/>
-	~~Description~~: ~~Flavin monooxygenase from Stenotrophomonas maltophilia~~. ~~Q193R H194T mutant~~	+	[[Category: Flavin-containing monooxygenase]]
		+	[[Category: Ali, S T.]]
		+	[[Category: Allen, M J.]]
		+	[[Category: Grogan, G.]]
		+	[[Category: Jensen, C N.]]
		+	[[Category: Oxidoreductase]]

OCA at 07:14, 29 September 2013

OCA — Sun, 29 Sep 2013 07:14:59 GMT

←Older revision		Revision as of 07:14, 29 September 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4c5o is ON HOLD ~~until sometime in the future~~	+	The entry 4c5o is ON HOLD

	Authors: Jensen, C.N., Ali, S.T., Allen, M.J., Grogan, G.		Authors: Jensen, C.N., Ali, S.T., Allen, M.J., Grogan, G.

	Description: Flavin monooxygenase from Stenotrophomonas maltophilia. Q193R H194T mutant		Description: Flavin monooxygenase from Stenotrophomonas maltophilia. Q193R H194T mutant

OCA: Protected "4c5o" [edit=sysop:move=sysop]

OCA — Fri, 20 Sep 2013 03:19:16 GMT

Protected "4c5o" [edit=sysop:move=sysop]

←Older revision

Revision as of 03:19, 20 September 2013

OCA: New page: '''Unreleased structure''' The entry 4c5o is ON HOLD until sometime in the future Authors: Jensen, C.N., Ali, S.T., Allen, M.J., Grogan, G. Description: Flavin monooxygenase from Steno...

OCA — Fri, 20 Sep 2013 03:19:15 GMT

New page: '''Unreleased structure''' The entry 4c5o is ON HOLD until sometime in the future Authors: Jensen, C.N., Ali, S.T., Allen, M.J., Grogan, G. Description: Flavin monooxygenase from Steno...

New page

'''Unreleased structure'''

The entry 4c5o is ON HOLD until sometime in the future

Authors: Jensen, C.N., Ali, S.T., Allen, M.J., Grogan, G.

Description: Flavin monooxygenase from Stenotrophomonas maltophilia. Q193R H194T mutant