2fmo - Revision history

OCA at 09:29, 30 August 2023

2023-08-30T09:29:11Z

← Older revision		Revision as of 09:29, 30 August 2023
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	<StructureSection load='2fmo' size='340' side='right'caption='[[2fmo]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='2fmo' size='340' side='right'caption='[[2fmo]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fmo]] is a 3 chain structure with sequence from [https://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=2FMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FMO FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fmo]] is a 3 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=2FMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FMO 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=MPD:(4S)-~~2~~-METHYL-2,4-PENTANEDIOL'>MPD</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]] 2.25Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[2fmn\|2fmn]]~~</~~div~~><~~/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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b></td><td class="sblockDat">metF~~ (~~[https://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~~'>[https://en.wikipedia.org/wiki/Methylenetetrahydrofolate_reductase_(NAD(P)H) Methylenetetrahydrofolate reductase (NAD(P)H)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.20 1.5.1.20] </~~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=2fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmo OCA], [https://pdbe.org/2fmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fmo RCSB], [https://www.ebi.ac.uk/pdbsum/2fmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fmo 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=2fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmo OCA], [https://pdbe.org/2fmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fmo RCSB], [https://www.ebi.ac.uk/pdbsum/2fmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fmo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/METF_ECOLI METF_ECOLI]] Methylenetetrahydrofolate reductase required to generate the methyl groups necessary for methionine synthetase to convert homocysteine to methionine.<ref>PMID:14275142</ref>		[https://www.uniprot.org/uniprot/METF_ECOLI METF_ECOLI] Methylenetetrahydrofolate reductase required to generate the methyl groups necessary for methionine synthetase to convert homocysteine to methionine.<ref>PMID:14275142</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</div>		</div>
	<div class="pdbe-citations 2fmo" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2fmo" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Methylenetetrahydrofolate reductase 3D structures\|Methylenetetrahydrofolate reductase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Bacillus~~ coli ~~migula 1895~~]]		[[Category: Escherichia coli]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Campbell, E]]		[[Category: Campbell E]]
	[[Category: Guenther~~, B D~~]]		[[Category: Guenther BD]]
	[[Category: Lennon~~, B W~~]]		[[Category: Lennon BW]]
	[[Category: Ludwig~~, M L~~]]		[[Category: Ludwig ML]]
	[[Category: Matthews~~, R G~~]]		[[Category: Matthews RG]]
	[[Category: Pejchal, R]]		[[Category: Pejchal R]]
	~~[[Category: Flavin]]~~
	~~[[Category: Oxidoreductase]]~~
	~~[[Category: Reductase]]~~
	~~[[Category: Tim barrel~~]]

OCA at 15:29, 3 March 2021

2021-03-03T15:29:35Z

← Older revision		Revision as of 15:29, 3 March 2021
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	==Ala177Val mutant of E. coli Methylenetetrahydrofolate Reductase==		==Ala177Val mutant of E. coli Methylenetetrahydrofolate Reductase==
	<StructureSection load='2fmo' size='340' side='right' caption='[[2fmo]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='2fmo' size='340' side='right'caption='[[2fmo]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fmo]] is a 3 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=2FMO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2FMO FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fmo]] is a 3 chain structure with sequence from [https://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=2FMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FMO 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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fmn\|2fmn]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2fmn\|2fmn]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">metF ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">metF ([https://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/Methylenetetrahydrofolate_reductase_(NAD(P)H) Methylenetetrahydrofolate reductase (NAD(P)H)], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.20 1.5.1.20] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methylenetetrahydrofolate_reductase_(NAD(P)H) Methylenetetrahydrofolate reductase (NAD(P)H)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.20 1.5.1.20] </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=2fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmo OCA], [~~http~~://pdbe.org/2fmo PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2fmo RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2fmo PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2fmo 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=2fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmo OCA], [https://pdbe.org/2fmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fmo RCSB], [https://www.ebi.ac.uk/pdbsum/2fmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fmo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/METF_ECOLI METF_ECOLI]] Methylenetetrahydrofolate reductase required to generate the methyl groups necessary for methionine synthetase to convert homocysteine to methionine.<ref>PMID:14275142</ref>		[[https://www.uniprot.org/uniprot/METF_ECOLI METF_ECOLI]] Methylenetetrahydrofolate reductase required to generate the methyl groups necessary for methionine synthetase to convert homocysteine to methionine.<ref>PMID:14275142</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</StructureSection>		</StructureSection>
	[[Category: Bacillus coli migula 1895]]		[[Category: Bacillus coli migula 1895]]
			[[Category: Large Structures]]
	[[Category: Campbell, E]]		[[Category: Campbell, E]]
	[[Category: Guenther, B D]]		[[Category: Guenther, B D]]

OCA at 08:59, 14 June 2018

2018-06-14T08:59:31Z

← Older revision		Revision as of 08:59, 14 June 2018
Line 1:		Line 1:

	==Ala177Val mutant of E. coli Methylenetetrahydrofolate Reductase==		==Ala177Val mutant of E. coli Methylenetetrahydrofolate Reductase==
	<StructureSection load='2fmo' size='340' side='right' caption='[[2fmo]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='2fmo' size='340' side='right' caption='[[2fmo]], [[Resolution\|resolution]] 2.25Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">metF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">metF ([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/Methylenetetrahydrofolate_reductase_(NAD(P)H) Methylenetetrahydrofolate reductase (NAD(P)H)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.20 1.5.1.20] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylenetetrahydrofolate_reductase_(NAD(P)H) Methylenetetrahydrofolate reductase (NAD(P)H)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.20 1.5.1.20] </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=2fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmo OCA], [http://pdbe.org/2fmo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fmo RCSB], [http://www.ebi.ac.uk/pdbsum/2fmo 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=2fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmo OCA], [http://pdbe.org/2fmo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fmo RCSB], [http://www.ebi.ac.uk/pdbsum/2fmo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fmo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/2fmo_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/2fmo_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fmo ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 00:47, 12 September 2015

2015-09-12T00:47:38Z

← Older revision		Revision as of 00:47, 12 September 2015
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	<StructureSection load='2fmo' size='340' side='right' caption='[[2fmo]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='2fmo' size='340' side='right' caption='[[2fmo]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fmo]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Escherichia_coli Escherichia~~ coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FMO FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fmo]] is a 3 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=2FMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FMO 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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fmn\|2fmn]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fmn\|2fmn]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">metF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 ~~Escherichia~~ coli])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">metF ([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/Methylenetetrahydrofolate_reductase_(NAD(P)H) Methylenetetrahydrofolate reductase (NAD(P)H)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.20 1.5.1.20] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylenetetrahydrofolate_reductase_(NAD(P)H) Methylenetetrahydrofolate reductase (NAD(P)H)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.20 1.5.1.20] </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=2fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fmo RCSB], [http://www.ebi.ac.uk/pdbsum/2fmo 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=2fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmo OCA], [http://pdbe.org/2fmo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fmo RCSB], [http://www.ebi.ac.uk/pdbsum/2fmo PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	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 2fmo" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Escherichia~~ coli]]		[[Category: Bacillus coli migula 1895]]
	[[Category: Campbell, E]]		[[Category: Campbell, E]]
	[[Category: Guenther, B D]]		[[Category: Guenther, B D]]

OCA at 21:35, 25 December 2014

2014-12-25T21:35:58Z

← Older revision		Revision as of 21:35, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fmo]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FMO FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fmo]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FMO FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fmn\|2fmn]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fmn\|2fmn]]</td></tr>
	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">metF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">metF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylenetetrahydrofolate_reductase_(NAD(P)H) Methylenetetrahydrofolate reductase (NAD(P)H)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.20 1.5.1.20] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylenetetrahydrofolate_reductase_(NAD(P)H) Methylenetetrahydrofolate reductase (NAD(P)H)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.20 1.5.1.20] </span></td></tr>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fmo RCSB], [http://www.ebi.ac.uk/pdbsum/2fmo 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=2fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fmo RCSB], [http://www.ebi.ac.uk/pdbsum/2fmo PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/METF_ECOLI METF_ECOLI]] Methylenetetrahydrofolate reductase required to generate the methyl groups necessary for methionine synthetase to convert homocysteine to methionine.<ref>PMID:14275142</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Campbell, E.]]		[[Category: Campbell, E]]
	[[Category: Guenther, B D.]]		[[Category: Guenther, B D]]
	[[Category: Lennon, B W.]]		[[Category: Lennon, B W]]
	[[Category: Ludwig, M L.]]		[[Category: Ludwig, M L]]
	[[Category: Matthews, R G.]]		[[Category: Matthews, R G]]
	[[Category: Pejchal, R.]]		[[Category: Pejchal, R]]
	[[Category: Flavin]]		[[Category: Flavin]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Reductase]]		[[Category: Reductase]]
	[[Category: Tim barrel]]		[[Category: Tim barrel]]

OCA at 08:49, 30 September 2014

2014-09-30T08:49:27Z

← Older revision		Revision as of 08:49, 30 September 2014
Line 1:		Line 1:
	[[Image:~~2fmo~~.~~png~~\|~~left~~\|~~200px~~]]		==Ala177Val mutant of E. coli Methylenetetrahydrofolate Reductase==
			<StructureSection load='2fmo' size='340' side='right' caption='[[2fmo]], [[Resolution\|resolution]] 2.25Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2fmo]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FMO FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2fmn\|2fmn]]</td></tr>
			<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">metF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylenetetrahydrofolate_reductase_(NAD(P)H) Methylenetetrahydrofolate reductase (NAD(P)H)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.20 1.5.1.20] </span></td></tr>
			<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fmo RCSB], [http://www.ebi.ac.uk/pdbsum/2fmo PDBsum]</span></td></tr>
			<table>
			== Evolutionary Conservation ==
			[[Image:Consurf_key_small.gif\|200px\|right]]
			Check<jmol>
			<jmolCheckbox>
			<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/2fmo_consurf.spt"</scriptWhenChecked>
			<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
			<text>to colour the structure by Evolutionary Conservation</text>
			</jmolCheckbox>
			</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
			<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			In human methylenetetrahydrofolate reductase (MTHFR) the Ala222Val (677C-->T) polymorphism encodes a heat-labile gene product that is associated with elevated levels of homocysteine and possibly with risk for cardiovascular disease. Generation of the equivalent Ala to Val mutation in Escherichia coli MTHFR, which is 30% identical to the catalytic domain of the human enzyme, creates a protein with enhanced thermolability. In both human and E. coli MTHFR, the A --> V mutation increases the rate of dissociation of FAD, and in both enzymes, loss of FAD is linked to changes in quaternary structure [Yamada, K., Chen, Z., Rozen, R., and Matthews, R. G. (2001) Proc. Natl. Acad. Sci. U.S.A. 98, 14853-14858; Guenther, B. D., Sheppard, C. A., Tran, P., Rozen, R., Matthews, R. G., and Ludwig, M. L. (1999) Nat. Struct. Biol. 6, 359-365]. Folates have been shown to protect both human and bacterial enzymes from loss of FAD. Despite its effect on affinity for FAD, the A --> V mutation is located at the bottom of the (betaalpha)(8) barrel of the catalytic domain in a position that does not contact the bound FAD prosthetic group. Here we report the structures of the Ala177Val mutant of E. coli MTHFR and of its complex with the 5,10-dideazafolate analogue, LY309887, and suggest mechanisms by which the mutation may perturb FAD binding. Helix alpha5, which immediately precedes the loop bearing the mutation, carries several residues that interact with FAD, including Asn168, Arg171, and Lys172. In the structures of the mutant enzyme this helix is displaced, perturbing protein-FAD interactions. In the complex with LY309887, the pterin-like ring of the analogue stacks against the si face of the flavin and is secured by hydrogen bonds to residues Gln183 and Asp120 that adjoin this face. The direct interactions of bound folate with the cofactor provide one mechanism for linkage between binding of FAD and folate binding that could account in part for the protective action of folates. Conformation changes induced by folate binding may also suppress dissociation of FAD.

	~~{{STRUCTURE_2fmo\| PDB=2fmo \| SCENE= }}~~		Structural perturbations in the Ala --> Val polymorphism of methylenetetrahydrofolate reductase: how binding of folates may protect against inactivation.,Pejchal R, Campbell E, Guenther BD, Lennon BW, Matthews RG, Ludwig ML Biochemistry. 2006 Apr 18;45(15):4808-18. PMID:16605249<ref>PMID:16605249</ref>

	~~===Ala177Val mutant~~ of E. ~~coli Methylenetetrahydrofolate Reductase===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_16605249}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[2fmo]] is a 3 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org~~/~~wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMO OCA].~~		</StructureSection>

	==~~Reference~~==
	<~~ref group="xtra">PMID:016605249<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Campbell, E.]]		[[Category: Campbell, E.]]

OCA: Protected "2fmo" [edit=sysop:move=sysop]

2013-01-07T13:46:11Z

Protected "2fmo" [edit=sysop:move=sysop]

← Older revision	Revision as of 13:46, 7 January 2013
(No difference)

OCA at 13:46, 7 January 2013

2013-01-07T13:46:08Z

← Older revision		Revision as of 13:46, 7 January 2013
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	~~{{Seed}}~~
	[[Image:2fmo.png\|left\|200px]]		[[Image:2fmo.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2fmo", creates the "Structure Box" on the page.~~
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~
	~~or leave the SCENE parameter empty for the default display.~~
	~~-->~~
	{{STRUCTURE_2fmo\| PDB=2fmo \| SCENE= }}		{{STRUCTURE_2fmo\| PDB=2fmo \| SCENE= }}

	===Ala177Val mutant of E. coli Methylenetetrahydrofolate Reductase===		===Ala177Val mutant of E. coli Methylenetetrahydrofolate Reductase===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_16605249}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 16605249 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_16605249}}		{{ABSTRACT_PUBMED_16605249}}

	==About this Structure==		==About this Structure==
	~~2FMO~~ is a 3 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMO OCA].		[[2fmo]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMO OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~16605249~~</ref><references group="xtra"/>		<ref group="xtra">PMID:016605249</ref><references group="xtra"/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	[[Category: Campbell, E.]]		[[Category: Campbell, E.]]
Line 35:		Line 23:
	[[Category: Reductase]]		[[Category: Reductase]]
	[[Category: Tim barrel]]		[[Category: Tim barrel]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:33:10 2009''~~

OCA at 06:33, 18 February 2009

2009-02-18T06:33:12Z

← Older revision		Revision as of 06:33, 18 February 2009
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
	2FMO is a ~~[[Single protein]]~~ structure of ~~sequence~~ from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMO OCA].		2FMO is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMO OCA].

	==Reference==		==Reference==
	Structural perturbations in the Ala --> Val polymorphism of methylenetetrahydrofolate reductase: how binding of folates may protect against inactivation., Pejchal R, Campbell E, Guenther BD, Lennon BW, Matthews RG, Ludwig ML, Biochemistry. 2006 Apr 18;45(15):4808-18. PMID:~~[http://www.ncbi.nlm.nih.gov~~/~~pubmed~~/~~16605249 16605249]~~		<ref group="xtra">PMID:16605249</ref><references group="xtra"/>
	[[Category: Escherichia coli]]		[[Category: Escherichia coli]]
	~~[[Category: Single protein]]~~
	[[Category: Campbell, E.]]		[[Category: Campbell, E.]]
	[[Category: Guenther, B D.]]		[[Category: Guenther, B D.]]
Line 37:		Line 36:
	[[Category: Tim barrel]]		[[Category: Tim barrel]]

	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Jul 29 14~~:49:~~19 2008~~''		''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 08:33:10 2009''

OCA at 11:49, 29 July 2008

2008-07-29T11:49:23Z

← Older revision		Revision as of 11:49, 29 July 2008
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	[[Image:2fmo.~~gif~~\|left\|200px]]		{{Seed}}
			[[Image:2fmo.png\|left\|200px]]

	<!--		<!--
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	{{STRUCTURE_2fmo\| PDB=2fmo \| SCENE= }}		{{STRUCTURE_2fmo\| PDB=2fmo \| SCENE= }}

	~~'''~~Ala177Val mutant of E. coli Methylenetetrahydrofolate Reductase~~'''~~		===Ala177Val mutant of E. coli Methylenetetrahydrofolate Reductase===


	~~==Overview==~~		<!--
	~~In human methylenetetrahydrofolate reductase (MTHFR) the Ala222Val (677C~~-->T) polymorphism encodes a heat-labile gene product that is associated with elevated levels of homocysteine and possibly with risk for cardiovascular disease. Generation of the equivalent Ala to Val mutation in Escherichia coli MTHFR, which is 30% identical to the catalytic domain of the human enzyme, ~~creates a protein with enhanced thermolability. In both human and E. coli MTHFR~~, the ~~A --> V mutation increases~~ the ~~rate of dissociation of FAD, and in both enzymes, loss of FAD is linked to changes in quaternary structure [Yamada, K., Chen, Z., Rozen, R., and Matthews, R. G.~~ (~~2001) Proc. Natl. Acad. Sci. U.S.A. 98, 14853-14858; Guenther, B. D., Sheppard, C. A., Tran, P., Rozen, R., Matthews, R~~. G.~~, and Ludwig, M. L. (1999~~) ~~Nat. Struct. Biol. 6~~, ~~359-365]. Folates have been shown to protect both human and bacterial enzymes from loss of FAD. Despite its effect on affinity for FAD, the A --> V mutation~~ is ~~located at~~ the ~~bottom of the (betaalpha)(8) barrel of the catalytic domain in a position that does not contact the bound FAD prosthetic group~~. ~~Here we report the structures of the Ala177Val mutant of E. coli MTHFR and of its complex with the 5,10~~-dideazafolate analogue, LY309887, and suggest mechanisms by which the mutation may perturb FAD binding. Helix alpha5, which immediately precedes the loop bearing the mutation, carries several residues that interact with FAD, including Asn168, Arg171, and Lys172. In the structures of the mutant enzyme this helix is displaced, perturbing protein-FAD interactions. In the complex with LY309887, the pterin-like ring of the analogue stacks against the si face of the flavin and is secured by hydrogen bonds to residues Gln183 and Asp120 that adjoin this face. The direct interactions of bound folate with the cofactor provide one mechanism for linkage between binding of FAD and folate binding that could account in part for the protective action of folates. Conformation changes induced by folate binding may also suppress dissociation of FAD.		The line below this paragraph, {{ABSTRACT_PUBMED_16605249}}, adds the Publication Abstract to the page
			(as it appears on PubMed at http://www.pubmed.gov), where 16605249 is the PubMed ID number.
			-->
			{{ABSTRACT_PUBMED_16605249}}

	==About this Structure==		==About this Structure==
Line 32:		Line 36:
	[[Category: Reductase]]		[[Category: Reductase]]
	[[Category: Tim barrel]]		[[Category: Tim barrel]]
	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 04~~:04:35 2008''
			''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:49:19 2008''