5ccc - Revision history

OCA at 08:36, 27 September 2023

2023-09-27T08:36:52Z

← Older revision		Revision as of 08:36, 27 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5ccc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CCC FirstGlance]. <br>		<table><tr><td colspan='2'>[[5ccc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CCC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DDF:5,10-DIDEAZATETRAHYDROFOLIC+ACID'>DDF</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 1.5Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DDF:5,10-DIDEAZATETRAHYDROFOLIC+ACID'>DDF</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=5ccc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccc OCA], [https://pdbe.org/5ccc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ccc RCSB], [https://www.ebi.ac.uk/pdbsum/5ccc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ccc 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=5ccc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccc OCA], [https://pdbe.org/5ccc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ccc RCSB], [https://www.ebi.ac.uk/pdbsum/5ccc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ccc ProSAT]</span></td></tr>
	</table>		</table>

OCA at 11:58, 14 June 2023

2023-06-14T11:58:17Z

← Older revision		Revision as of 11:58, 14 June 2023
Line 3:		Line 3:
	<StructureSection load='5ccc' size='340' side='right'caption='[[5ccc]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='5ccc' size='340' side='right'caption='[[5ccc]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5ccc]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"bacillus_coli"_migula_1895 "bacillus~~ coli~~" migula 1895~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5CCC FirstGlance]. <br>		<table><tr><td colspan='2'>[[5ccc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CCC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DDF:5,10-DIDEAZATETRAHYDROFOLIC+ACID'>DDF</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene~~></td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DDF:5,10-DIDEAZATETRAHYDROFOLIC+ACID'>DDF</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5cc9\|5cc9]]</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=5ccc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccc OCA], [https://pdbe.org/5ccc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ccc RCSB], [https://www.ebi.ac.uk/pdbsum/5ccc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ccc ProSAT]</span></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">folA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </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=5ccc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccc OCA], [~~http~~://pdbe.org/5ccc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5ccc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5ccc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5ccc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/~~DYR_ECOL6 DYR_ECOL6]~~] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis ~~(By similarity)~~.		[https://www.uniprot.org/uniprot/DYR_ECOLI DYR_ECOLI] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
	<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: ~~Bacillus~~ coli ~~migula 1895]]~~		[[Category: Escherichia coli]]
	~~[[Category: Dihydrofolate reductase~~]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Oyen, D]]		[[Category: Oyen D]]
	[[Category: Wright~~, P E]]~~		[[Category: Wright PE]]
	~~[[Category: Folate metabolism]]~~
	~~[[Category: Oxidoreductase~~]]

OCA at 11:12, 25 December 2019

2019-12-25T11:12:56Z

← Older revision		Revision as of 11:12, 25 December 2019
Line 1:		Line 1:

	==wild-type E.coli dihydrofolate reductase complexed with 5,10-dideazatetrahydrofolate and oxidized nicotinamide adenine dinucleotide phosphate==		==wild-type E.coli dihydrofolate reductase complexed with 5,10-dideazatetrahydrofolate and oxidized nicotinamide adenine dinucleotide phosphate==
	<StructureSection load='5ccc' size='340' side='right' caption='[[5ccc]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='5ccc' size='340' side='right'caption='[[5ccc]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5ccc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CCC FirstGlance]. <br>		<table><tr><td colspan='2'>[[5ccc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CCC FirstGlance]. <br>
Line 21:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 5ccc" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5ccc" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Dihydrofolate reductase 3D structures\|Dihydrofolate reductase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 27:		Line 30:
	[[Category: Bacillus coli migula 1895]]		[[Category: Bacillus coli migula 1895]]
	[[Category: Dihydrofolate reductase]]		[[Category: Dihydrofolate reductase]]
			[[Category: Large Structures]]
	[[Category: Oyen, D]]		[[Category: Oyen, D]]
	[[Category: Wright, P E]]		[[Category: Wright, P E]]
	[[Category: Folate metabolism]]		[[Category: Folate metabolism]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 12:26, 6 November 2017

2017-11-06T12:26:49Z

← Older revision		Revision as of 12:26, 6 November 2017
Line 3:		Line 3:
	<StructureSection load='5ccc' size='340' side='right' caption='[[5ccc]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='5ccc' size='340' side='right' caption='[[5ccc]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5ccc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CCC FirstGlance]. <br>		<table><tr><td colspan='2'>[[5ccc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CCC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DDF:5,10-DIDEAZATETRAHYDROFOLIC+ACID'>DDF</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DDF:5,10-DIDEAZATETRAHYDROFOLIC+ACID'>DDF</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5cc9\|5cc9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5cc9\|5cc9]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">folA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </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=5ccc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccc OCA], [http://pdbe.org/5ccc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ccc RCSB], [http://www.ebi.ac.uk/pdbsum/5ccc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ccc 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=5ccc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccc OCA], [http://pdbe.org/5ccc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ccc RCSB], [http://www.ebi.ac.uk/pdbsum/5ccc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ccc ProSAT]</span></td></tr>
Line 20:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 5ccc" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5ccc" style="background-color:#fffaf0;"></div>

	~~==See Also==~~
	*[[Dihydrofolate reductase\|Dihydrofolate reductase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Bacillus coli migula 1895]]
	[[Category: Dihydrofolate reductase]]		[[Category: Dihydrofolate reductase]]
	[[Category: Oyen, D]]		[[Category: Oyen, D]]

OCA at 16:08, 17 May 2017

2017-05-17T16:08:17Z

← Older revision		Revision as of 16:08, 17 May 2017
Line 1:		Line 1:

	==wild-type E.coli dihydrofolate reductase complexed with 5,10-dideazatetrahydrofolate and oxidized nicotinamide adenine dinucleotide phosphate==		==wild-type E.coli dihydrofolate reductase complexed with 5,10-dideazatetrahydrofolate and oxidized nicotinamide adenine dinucleotide phosphate==
	<StructureSection load='5ccc' size='340' side='right' caption='[[5ccc]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='5ccc' size='340' side='right' caption='[[5ccc]], [[Resolution\|resolution]] 1.50Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5cc9\|5cc9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5cc9\|5cc9]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </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=5ccc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5ccc RCSB], [http://www.ebi.ac.uk/pdbsum/5ccc 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=5ccc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccc OCA], [http://pdbe.org/5ccc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ccc RCSB], [http://www.ebi.ac.uk/pdbsum/5ccc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ccc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 5ccc" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Dihydrofolate reductase\|Dihydrofolate reductase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 20:01, 5 August 2015

2015-08-05T20:01:44Z

← Older revision		Revision as of 20:01, 5 August 2015
Line 1:		Line 1:
	'''~~Unreleased~~ structure'''		==wild-type E.coli dihydrofolate reductase complexed with 5,10-dideazatetrahydrofolate and oxidized nicotinamide adenine dinucleotide phosphate==
			<StructureSection load='5ccc' size='340' side='right' caption='[[5ccc]], [[Resolution\|resolution]] 1.50Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[5ccc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CCC FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DDF:5,10-DIDEAZATETRAHYDROFOLIC+ACID'>DDF</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5cc9\|5cc9]]</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </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=5ccc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5ccc RCSB], [http://www.ebi.ac.uk/pdbsum/5ccc PDBsum]</span></td></tr>
			</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/DYR_ECOL6 DYR_ECOL6]] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The enzyme dihydrofolate reductase (DHFR, E) from Escherichia coli is a paradigm for the role of protein dynamics in enzyme catalysis. Previous studies have shown that the enzyme progresses through the kinetic cycle by modulating the dynamic conformational landscape in the presence of substrate dihydrofolate (DHF), product tetrahydrofolate (THF), and cofactor (NADPH or NADP(+)). This study focuses on the quantitative description of the relationship between protein fluctuations and product release, the rate-limiting step of DHFR catalysis. NMR relaxation dispersion measurements of millisecond time scale motions for the E:THF:NADP(+) and E:THF:NADPH complexes of wild-type and the Leu28Phe (L28F) point mutant reveal conformational exchange between an occluded ground state and a low population of a closed state. The backbone structures of the occluded ground states of the wild-type and mutant proteins are very similar, but the rates of exchange with the closed excited states are very different. Integrated analysis of relaxation dispersion data and THF dissociation rates measured by stopped-flow spectroscopy shows that product release can occur by two pathways. The intrinsic pathway consists of spontaneous product dissociation and occurs for all THF-bound complexes of DHFR. The allosteric pathway features cofactor-assisted product release from the closed excited state and is utilized only in the E:THF:NADPH complexes. The L28F mutation alters the partitioning between the pathways and results in increased flux through the intrinsic pathway relative to the wild-type enzyme. This repartitioning could represent a general mechanism to explain changes in product release rates in other E. coli DHFR mutants.

	~~The entry 5ccc is ON HOLD~~		Cofactor-Mediated Conformational Dynamics Promote Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway.,Oyen D, Fenwick RB, Stanfield RL, Dyson HJ, Wright PE J Am Chem Soc. 2015 Jul 29;137(29):9459-68. doi: 10.1021/jacs.5b05707. Epub 2015 , Jul 14. PMID:26147643<ref>PMID:26147643</ref>

	~~Authors: Oyen~~, D.~~, Wright, P~~.E.		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~Description: wild-type E.coli dihydrofolate reductase complexed with 5,10-dideazatetrahydrofolate and oxidized nicotinamide adenine dinucleotide phosphate~~		== References ==
	~~[[Category: Unreleased Structures]]~~		<references/>
	[[Category: ~~Wright, P.E~~]]		__TOC__
			</StructureSection>
			[[Category: Dihydrofolate reductase]]
	[[Category: Oyen, D]]		[[Category: Oyen, D]]
			[[Category: Wright, P E]]
			[[Category: Folate metabolism]]
			[[Category: Oxidoreductase]]

OCA: Protected "5ccc" [edit=sysop:move=sysop]

2015-07-08T13:59:33Z

Protected "5ccc" [edit=sysop:move=sysop]

← Older revision	Revision as of 13:59, 8 July 2015
(No difference)

OCA: New page: '''Unreleased structure''' The entry 5ccc is ON HOLD Authors: Oyen, D., Wright, P.E. Description: wild-type E.coli dihydrofolate reductase complexed with 5,10-dideazatetrahydrofolate a...

2015-07-08T13:59:32Z

New page: '''Unreleased structure''' The entry 5ccc is ON HOLD Authors: Oyen, D., Wright, P.E. Description: wild-type E.coli dihydrofolate reductase complexed with 5,10-dideazatetrahydrofolate a...

New page

'''Unreleased structure'''

The entry 5ccc is ON HOLD

Authors: Oyen, D., Wright, P.E.

Description: wild-type E.coli dihydrofolate reductase complexed with 5,10-dideazatetrahydrofolate and oxidized nicotinamide adenine dinucleotide phosphate
[[Category: Unreleased Structures]]
[[Category: Wright, P.E]]
[[Category: Oyen, D]]