6dqo - Revision history

OCA at 14:32, 6 March 2024

OCA — Wed, 06 Mar 2024 14:32:50 GMT

←Older revision		Revision as of 14:32, 6 March 2024
Line 3:		Line 3:
	<StructureSection load='6dqo' size='340' side='right'caption='[[6dqo]], [[Resolution\|resolution]] 1.71Å' scene=''>		<StructureSection load='6dqo' size='340' side='right'caption='[[6dqo]], [[Resolution\|resolution]] 1.71Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6dqo]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Ecoli Ecoli~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DQO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6DQO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6dqo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DQO FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat"~~><scene name~~=~~'pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene~~>, ~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.705Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>ssuE, ycbP, b0937, JW0920 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~83333 ECOLI])</td~~><~~/tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[http://en.wikipedia.org/wiki/FMN_reductase_(NADPH) FMN reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.38 1.5.1.38]~~ </~~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=6dqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dqo OCA], [https://pdbe.org/6dqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dqo RCSB], [https://www.ebi.ac.uk/pdbsum/6dqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dqo 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=6dqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dqo OCA], [~~http~~://pdbe.org/6dqo PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6dqo RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6dqo PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6dqo ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SSUE_ECOLI SSUE_ECOLI]] Catalyzes an NADPH-dependent reduction of FMN, but is also able to reduce FAD or riboflavin.	+	[https://www.uniprot.org/uniprot/SSUE_ECOLI SSUE_ECOLI] Catalyzes an NADPH-dependent reduction of FMN, but is also able to reduce FAD or riboflavin.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The pi-helix located at the tetramer interface of two-component FMN-dependent reductases contributes to the structural divergence from canonical FMN-bound reductases within the NADPH:FMN reductase family. The pi-helix in the SsuE FMN-dependent reductase of the alkanesulfonate monooxygenase system has been proposed to be generated by the insertion of a Tyr residue in the conserved alpha4-helix. Variants of Tyr118 were generated, and their X-ray crystal structures determined, to evaluate how these alterations affect the structural integrity of the pi-helix. The structure of the Y118A SsuE pi-helix was converted to an alpha-helix, similar to the FMN-bound members of the NADPH:FMN reductase family. Although the pi-helix was altered, the FMN binding region remained unchanged. Conversely, deletion of Tyr118 disrupted the secondary structural properties of the pi-helix, generating a random coil region in the middle of helix 4. Both the Y118A and Delta118 SsuE SsuE variants crystallize as a dimer. The MsuE FMN reductase involved in the desulfonation of methanesulfonates is structurally similar to SsuE, but the pi-helix contains a His insertional residue. Exchanging the pi-helix insertional residue of each enzyme did not result in equivalent kinetic properties. Structure-based sequence analysis further demonstrated the presence of a similar Tyr residue in an FMN-bound reductase in the NADPH:FMN reductase family that is not sufficient to generate a pi-helix. Results from the structural and functional studies of the FMN-dependent reductases suggest that the insertional residue alone is not solely responsible for generating the pi-helix, and additional structural adaptions occur to provide the altered gain of function.	+
-		+
-	Not as easy as pi: An insertional residue does not explain the pi-helix gain-of-function in two-component FMN reductases.,McFarlane JS, Hagen RA, Chilton AS, Forbes DL, Lamb AL, Ellis HR Protein Sci. 2019 Jan;28(1):123-134. doi: 10.1002/pro.3504. Epub 2018 Nov 15. PMID:30171650<ref>PMID:30171650</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 6dqo" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ecoli~~]]	+	[[Category: Escherichia coli K-12]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Ellis~~, H R~~]]	+	[[Category: Ellis HR]]
-	[[Category: Lamb~~, A L~~]]	+	[[Category: Lamb AL]]
-	[[Category: McFarlane~~, J S]]~~	+	[[Category: McFarlane JS]]
-	~~[[Category: Flavoprotein]]~~	+
-	~~[[Category: Fmn]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Reductase~~]]	+

OCA at 08:33, 27 November 2019

OCA — Wed, 27 Nov 2019 08:33:49 GMT

←Older revision		Revision as of 08:33, 27 November 2019
Line 1:		Line 1:

	==Crystal structure of SsuE FMN reductase Y118A mutant in FMN bound form.==		==Crystal structure of SsuE FMN reductase Y118A mutant in FMN bound form.==
-	<StructureSection load='6dqo' size='340' side='right' caption='[[6dqo]], [[Resolution\|resolution]] 1.71Å' scene=''>	+	<StructureSection load='6dqo' size='340' side='right'caption='[[6dqo]], [[Resolution\|resolution]] 1.71Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6dqo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DQO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6dqo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DQO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ssuE, ycbP, b0937, JW0920 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/FMN_reductase_(NADPH) FMN reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.38 1.5.1.38] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/FMN_reductase_(NADPH) FMN reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.38 1.5.1.38] </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=6dqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dqo OCA], [http://pdbe.org/6dqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dqo RCSB], [http://www.ebi.ac.uk/pdbsum/6dqo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dqo 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=6dqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dqo OCA], [http://pdbe.org/6dqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dqo RCSB], [http://www.ebi.ac.uk/pdbsum/6dqo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dqo ProSAT]</span></td></tr>
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Ecoli]]
		+	[[Category: Large Structures]]
	[[Category: Ellis, H R]]		[[Category: Ellis, H R]]
	[[Category: Lamb, A L]]		[[Category: Lamb, A L]]

OCA at 06:35, 9 January 2019

OCA — Wed, 09 Jan 2019 06:35:30 GMT

←Older revision		Revision as of 06:35, 9 January 2019
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6dqo is ~~ON HOLD until Paper~~ Publication	+	==Crystal structure of SsuE FMN reductase Y118A mutant in FMN bound form.==
		+	<StructureSection load='6dqo' size='340' side='right' caption='[[6dqo]], [[Resolution\|resolution]] 1.71Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6dqo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DQO FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/FMN_reductase_(NADPH) FMN reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.38 1.5.1.38] </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=6dqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dqo OCA], [http://pdbe.org/6dqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dqo RCSB], [http://www.ebi.ac.uk/pdbsum/6dqo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dqo ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SSUE_ECOLI SSUE_ECOLI]] Catalyzes an NADPH-dependent reduction of FMN, but is also able to reduce FAD or riboflavin.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The pi-helix located at the tetramer interface of two-component FMN-dependent reductases contributes to the structural divergence from canonical FMN-bound reductases within the NADPH:FMN reductase family. The pi-helix in the SsuE FMN-dependent reductase of the alkanesulfonate monooxygenase system has been proposed to be generated by the insertion of a Tyr residue in the conserved alpha4-helix. Variants of Tyr118 were generated, and their X-ray crystal structures determined, to evaluate how these alterations affect the structural integrity of the pi-helix. The structure of the Y118A SsuE pi-helix was converted to an alpha-helix, similar to the FMN-bound members of the NADPH:FMN reductase family. Although the pi-helix was altered, the FMN binding region remained unchanged. Conversely, deletion of Tyr118 disrupted the secondary structural properties of the pi-helix, generating a random coil region in the middle of helix 4. Both the Y118A and Delta118 SsuE SsuE variants crystallize as a dimer. The MsuE FMN reductase involved in the desulfonation of methanesulfonates is structurally similar to SsuE, but the pi-helix contains a His insertional residue. Exchanging the pi-helix insertional residue of each enzyme did not result in equivalent kinetic properties. Structure-based sequence analysis further demonstrated the presence of a similar Tyr residue in an FMN-bound reductase in the NADPH:FMN reductase family that is not sufficient to generate a pi-helix. Results from the structural and functional studies of the FMN-dependent reductases suggest that the insertional residue alone is not solely responsible for generating the pi-helix, and additional structural adaptions occur to provide the altered gain of function.

-	~~Authors~~: McFarlane, ~~J.S.~~, ~~Ellis~~, ~~H.R.~~, Lamb, A.L.	+	Not as easy as pi: An insertional residue does not explain the pi-helix gain-of-function in two-component FMN reductases.,McFarlane JS, Hagen RA, Chilton AS, Forbes DL, Lamb AL, Ellis HR Protein Sci. 2019 Jan;28(1):123-134. doi: 10.1002/pro.3504. Epub 2018 Nov 15. PMID:30171650<ref>PMID:30171650</ref>

-	~~Description: Crystal structure~~ of ~~SsuE FMN reductase Y118A mutant in FMN bound form~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
-	[[Category: Lamb, A.L]]	+	<div class="pdbe-citations 6dqo" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Ellis~~, ~~H.R~~]]	+	== References ==
-	[[Category: ~~Mcfarlane, J.S~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Ellis, H R]]
		+	[[Category: Lamb, A L]]
		+	[[Category: McFarlane, J S]]
		+	[[Category: Flavoprotein]]
		+	[[Category: Fmn]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Reductase]]

OCA at 05:40, 4 July 2018

OCA — Wed, 04 Jul 2018 05:40:32 GMT

←Older revision		Revision as of 05:40, 4 July 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6dqo is ON HOLD	+	The entry 6dqo is ON HOLD until Paper Publication

	Authors: McFarlane, J.S., Ellis, H.R., Lamb, A.L.		Authors: McFarlane, J.S., Ellis, H.R., Lamb, A.L.

OCA: Protected "6dqo" [edit=sysop:move=sysop]

OCA — Wed, 20 Jun 2018 04:09:15 GMT

Protected "6dqo" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:09, 20 June 2018

OCA: New page: '''Unreleased structure''' The entry 6dqo is ON HOLD Authors: McFarlane, J.S., Ellis, H.R., Lamb, A.L. Description: Crystal structure of SsuE FMN reductase Y118A mutant in FMN bound fo...

OCA — Wed, 20 Jun 2018 04:09:12 GMT

New page: '''Unreleased structure''' The entry 6dqo is ON HOLD Authors: McFarlane, J.S., Ellis, H.R., Lamb, A.L. Description: Crystal structure of SsuE FMN reductase Y118A mutant in FMN bound fo...

New page

'''Unreleased structure'''

The entry 6dqo is ON HOLD

Authors: McFarlane, J.S., Ellis, H.R., Lamb, A.L.

Description: Crystal structure of SsuE FMN reductase Y118A mutant in FMN bound form.
[[Category: Unreleased Structures]]
[[Category: Lamb, A.L]]
[[Category: Ellis, H.R]]
[[Category: Mcfarlane, J.S]]