2fvx - Revision history

OCA at 09:25, 14 February 2024

2024-02-14T09:25:35Z

← Older revision		Revision as of 09:25, 14 February 2024
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	<StructureSection load='2fvx' size='340' side='right'caption='[[2fvx]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='2fvx' size='340' side='right'caption='[[2fvx]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fvx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"clostridium_rubrum"_ng_and_vaughn_1963 "clostridium rubrum" ng and vaughn 1963~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FVX FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fvx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FVX FirstGlance]. <br>
	</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></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]] 1.8Å</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></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=2fvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fvx OCA], [https://pdbe.org/2fvx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fvx RCSB], [https://www.ebi.ac.uk/pdbsum/2fvx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fvx 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=2fvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fvx OCA], [https://pdbe.org/2fvx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fvx RCSB], [https://www.ebi.ac.uk/pdbsum/2fvx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fvx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/FLAV_CLOBE FLAV_CLOBE]] Low-potential electron donor to a number of redox enzymes.		[https://www.uniprot.org/uniprot/FLAV_CLOBE FLAV_CLOBE] Low-potential electron donor to a number of redox enzymes.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=2fvx 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=2fvx ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	X-ray analyses of wild-type and mutant flavodoxins from Clostridium beijerinckii show that the conformation of the peptide Gly57-Asp58, in a bend near the isoalloxazine ring of FMN, is correlated with the oxidation state of the FMN prosthetic group. The Gly-Asp peptide may adopt any of three conformations: trans O-up, in which the carbonyl oxygen of Gly57 (O57) points toward the flavin ring; trans O-down, in which O57 points away from the flavin; and cis O-down. Interconversions among these conformers that are linked to oxidation-reduction of the flavin can modulate the redox potentials of bound FMN. In the semiquinone and reduced forms of the protein, the Gly57-Asp58 peptide adopts the trans O-up conformation and accepts a hydrogen bond from the flavin N5H [Smith, W. W., Burnett, R. M., Darling, G. D., & Ludwig, M. L. (1977) J. Mol. Biol. 117, 195-225; Ludwig, M. L., & Luschinsky, C. L. (1992) in Chemistry and Biochemistry of Flavoenzymes III (Muller, F., Ed.) pp 427-466, CRC Press, Boca Raton, FL]. Analyses reported in this paper confirm that, in crystals of wild-type oxidized C. beijerinckii flavodoxin, the Gly57-Asp58 peptide adopts the O-down orientation and isomerizes to the cis conformation. This cis form is preferentially stabilized in the crystals by intermolecular hydrogen bonding to Asn137. Structures for the mutant Asn137Ala indicate that a mixture of all three conformers, mostly O-down, exists in oxidized C. beijerinckii flavodoxin in the absence of intermolecular hydrogen bonds. Redox potentials have been manipulated by substitutions that alter the conformational energies of the bend at 56M-G-D-E. The mutation Asp58Pro was constructed to study a case where energies for cis-trans conversion would be different from that of wild type. Intermolecular interactions with Asn137 are precluded in the crystal, yet Gly57-Pro58 is cis, and O-down, when the flavin is oxidized. Reduction of the flavin induces rearrangement to the trans O-up conformation. Redox potential shifts reflect the altered energies associated with the peptide rearrangement; E(ox/sq) decreases by approximately 60 mV (1.3 kcal/mol). Further, the results of mutation of Gly57 agree with predictions that a side chain at residue 57 should make addition of the first electron more difficult, by raising the energy of the O-up conformer that forms when the flavin is reduced to its semiquinone state. The ox/sq potentials in the mutants Gly57Ala, Gly57Asn, and Gly57Asp are all decreased by approximately 60 mV (1.3 kcal/mol). Introduction of the beta-branched threonine side chain at position 57 has much larger effects on the conformations and potentials. The Thr57-Asp58 peptide adopts a trans O-down conformation when the flavin is oxidized; upon reduction to the semiquinone, the 57-58 peptide rotates to a trans O-up conformation resembling that found in the wild-type protein. Changes in FMN-protein interactions and in conformational equilibria in G57T combine to decrease the redox potential for the ox/sq equilibrium by 180 mV (+4.0 kcal/mol) and to increase the sq/hq potential by 80 mV (-1.7 kcal/mol). A thermodynamic scheme is introduced as a framework for rationalizing the properties of wild-type flavodoxin and the effects of the mutations.

	Control of oxidation-reduction potentials in flavodoxin from Clostridium beijerinckii: the role of conformation changes.,Ludwig ML, Pattridge KA, Metzger AL, Dixon MM, Eren M, Feng Y, Swenson RP Biochemistry. 1997 Feb 11;36(6):1259-80. PMID:9063874<ref>PMID:9063874</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 2fvx" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Flavodoxin 3D structures\|Flavodoxin 3D structures]]		*[[Flavodoxin 3D structures\|Flavodoxin 3D structures]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Clostridium ~~rubrum ng and vaughn 1963~~]]		[[Category: Clostridium beijerinckii]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Dixon~~, M M~~]]		[[Category: Dixon MM]]
	[[Category: Eren, M]]		[[Category: Eren M]]
	[[Category: Feng, Y]]		[[Category: Feng Y]]
	[[Category: Ludwig~~, M L~~]]		[[Category: Ludwig ML]]
	[[Category: Metzger~~, A L~~]]		[[Category: Metzger AL]]
	[[Category: Pattridge~~, K A~~]]		[[Category: Pattridge KA]]
	[[Category: Swenson, R]]		[[Category: Swenson R]]
	~~[[Category: Electron transport]]~~
	~~[[Category: Flavoprotein]]~~
	~~[[Category: Fmn~~]]

OCA at 15:41, 3 November 2021

2021-11-03T15:41:50Z

← Older revision		Revision as of 15:41, 3 November 2021
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	<StructureSection load='2fvx' size='340' side='right'caption='[[2fvx]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='2fvx' size='340' side='right'caption='[[2fvx]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fvx]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"clostridium_rubrum"_ng_and_vaughn_1963 "clostridium rubrum" ng and vaughn 1963]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2FVX FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fvx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"clostridium_rubrum"_ng_and_vaughn_1963 "clostridium rubrum" ng and vaughn 1963]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FVX 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></td></tr>		</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></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=2fvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fvx OCA], [~~http~~://pdbe.org/2fvx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2fvx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2fvx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2fvx 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=2fvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fvx OCA], [https://pdbe.org/2fvx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fvx RCSB], [https://www.ebi.ac.uk/pdbsum/2fvx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fvx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/FLAV_CLOBE FLAV_CLOBE]] Low-potential electron donor to a number of redox enzymes.		[[https://www.uniprot.org/uniprot/FLAV_CLOBE FLAV_CLOBE]] Low-potential electron donor to a number of redox enzymes.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 11:06, 27 March 2020

2020-03-27T11:06:16Z

← Older revision		Revision as of 11:06, 27 March 2020
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	==CLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: G57T REDUCED (277K)==		==CLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: G57T REDUCED (277K)==
	<StructureSection load='2fvx' size='340' side='right' caption='[[2fvx]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='2fvx' size='340' side='right'caption='[[2fvx]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fvx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"clostridium_rubrum"_ng_and_vaughn_1963 "clostridium rubrum" ng and vaughn 1963]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FVX FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fvx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"clostridium_rubrum"_ng_and_vaughn_1963 "clostridium rubrum" ng and vaughn 1963]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FVX FirstGlance]. <br>
Line 30:		Line 30:

	==See Also==		==See Also==
	*[[Flavodoxin\|Flavodoxin]]		*[[Flavodoxin 3D structures\|Flavodoxin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Clostridium rubrum ng and vaughn 1963]]		[[Category: Clostridium rubrum ng and vaughn 1963]]
			[[Category: Large Structures]]
	[[Category: Dixon, M M]]		[[Category: Dixon, M M]]
	[[Category: Eren, M]]		[[Category: Eren, M]]

OCA at 06:50, 20 June 2018

2018-06-20T06:50:18Z

← Older revision		Revision as of 06:50, 20 June 2018
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	==CLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: G57T REDUCED (277K)==		==CLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: G57T REDUCED (277K)==
	<StructureSection load='2fvx' size='340' side='right' caption='[[2fvx]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='2fvx' size='340' side='right' caption='[[2fvx]], [[Resolution\|resolution]] 1.80Å' scene=''>
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	<table><tr><td colspan='2'>[[2fvx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"clostridium_rubrum"_ng_and_vaughn_1963 "clostridium rubrum" ng and vaughn 1963]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FVX FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fvx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"clostridium_rubrum"_ng_and_vaughn_1963 "clostridium rubrum" ng and vaughn 1963]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FVX 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></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></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=2fvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fvx OCA], [http://pdbe.org/2fvx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fvx RCSB], [http://www.ebi.ac.uk/pdbsum/2fvx 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=2fvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fvx OCA], [http://pdbe.org/2fvx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fvx RCSB], [http://www.ebi.ac.uk/pdbsum/2fvx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fvx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 12:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fv/2fvx_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fv/2fvx_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>

OCA at 07:28, 9 February 2016

2016-02-09T07:28:11Z

← Older revision		Revision as of 07:28, 9 February 2016
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	<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=2fvx ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 19:58, 10 September 2015

2015-09-10T19:58:33Z

← Older revision		Revision as of 19:58, 10 September 2015
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	<StructureSection load='2fvx' size='340' side='right' caption='[[2fvx]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='2fvx' size='340' side='right' caption='[[2fvx]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fvx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Clostridium_beijerinckii Clostridium beijerinckii~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FVX FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fvx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"clostridium_rubrum"_ng_and_vaughn_1963 "clostridium rubrum" ng and vaughn 1963]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FVX 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></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></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=2fvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fvx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fvx RCSB], [http://www.ebi.ac.uk/pdbsum/2fvx 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=2fvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fvx OCA], [http://pdbe.org/2fvx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fvx RCSB], [http://www.ebi.ac.uk/pdbsum/2fvx PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 26:		Line 26:
	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 2fvx" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 33:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Clostridium ~~beijerinckii~~]]		[[Category: Clostridium rubrum ng and vaughn 1963]]
	[[Category: Dixon, M M]]		[[Category: Dixon, M M]]
	[[Category: Eren, M]]		[[Category: Eren, M]]

OCA at 05:21, 25 December 2014

2014-12-25T05:21:37Z

← Older revision		Revision as of 05:21, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2fvx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FVX FirstGlance]. <br>		<table><tr><td colspan='2'>[[2fvx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FVX FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene><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></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=2fvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fvx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fvx RCSB], [http://www.ebi.ac.uk/pdbsum/2fvx 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=2fvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fvx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fvx RCSB], [http://www.ebi.ac.uk/pdbsum/2fvx PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/FLAV_CLOBE FLAV_CLOBE]] Low-potential electron donor to a number of redox enzymes.
	== 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: Clostridium beijerinckii]]		[[Category: Clostridium beijerinckii]]
	[[Category: Dixon, M M.]]		[[Category: Dixon, M M]]
	[[Category: Eren, M.]]		[[Category: Eren, M]]
	[[Category: Feng, Y.]]		[[Category: Feng, Y]]
	[[Category: Ludwig, M L.]]		[[Category: Ludwig, M L]]
	[[Category: Metzger, A L.]]		[[Category: Metzger, A L]]
	[[Category: Pattridge, K A.]]		[[Category: Pattridge, K A]]
	[[Category: Swenson, R.]]		[[Category: Swenson, R]]
	[[Category: Electron transport]]		[[Category: Electron transport]]
	[[Category: Flavoprotein]]		[[Category: Flavoprotein]]
	[[Category: Fmn]]		[[Category: Fmn]]

OCA at 05:02, 29 September 2014

2014-09-29T05:02:40Z

← Older revision		Revision as of 05:02, 29 September 2014
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	[[Image:~~2fvx~~.~~png~~\|~~left~~\|~~200px~~]]		==CLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: G57T REDUCED (277K)==
			<StructureSection load='2fvx' size='340' side='right' caption='[[2fvx]], [[Resolution\|resolution]] 1.80Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2fvx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FVX FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene><br>
			<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=2fvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fvx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fvx RCSB], [http://www.ebi.ac.uk/pdbsum/2fvx 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/fv/2fvx_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 ==
			X-ray analyses of wild-type and mutant flavodoxins from Clostridium beijerinckii show that the conformation of the peptide Gly57-Asp58, in a bend near the isoalloxazine ring of FMN, is correlated with the oxidation state of the FMN prosthetic group. The Gly-Asp peptide may adopt any of three conformations: trans O-up, in which the carbonyl oxygen of Gly57 (O57) points toward the flavin ring; trans O-down, in which O57 points away from the flavin; and cis O-down. Interconversions among these conformers that are linked to oxidation-reduction of the flavin can modulate the redox potentials of bound FMN. In the semiquinone and reduced forms of the protein, the Gly57-Asp58 peptide adopts the trans O-up conformation and accepts a hydrogen bond from the flavin N5H [Smith, W. W., Burnett, R. M., Darling, G. D., & Ludwig, M. L. (1977) J. Mol. Biol. 117, 195-225; Ludwig, M. L., & Luschinsky, C. L. (1992) in Chemistry and Biochemistry of Flavoenzymes III (Muller, F., Ed.) pp 427-466, CRC Press, Boca Raton, FL]. Analyses reported in this paper confirm that, in crystals of wild-type oxidized C. beijerinckii flavodoxin, the Gly57-Asp58 peptide adopts the O-down orientation and isomerizes to the cis conformation. This cis form is preferentially stabilized in the crystals by intermolecular hydrogen bonding to Asn137. Structures for the mutant Asn137Ala indicate that a mixture of all three conformers, mostly O-down, exists in oxidized C. beijerinckii flavodoxin in the absence of intermolecular hydrogen bonds. Redox potentials have been manipulated by substitutions that alter the conformational energies of the bend at 56M-G-D-E. The mutation Asp58Pro was constructed to study a case where energies for cis-trans conversion would be different from that of wild type. Intermolecular interactions with Asn137 are precluded in the crystal, yet Gly57-Pro58 is cis, and O-down, when the flavin is oxidized. Reduction of the flavin induces rearrangement to the trans O-up conformation. Redox potential shifts reflect the altered energies associated with the peptide rearrangement; E(ox/sq) decreases by approximately 60 mV (1.3 kcal/mol). Further, the results of mutation of Gly57 agree with predictions that a side chain at residue 57 should make addition of the first electron more difficult, by raising the energy of the O-up conformer that forms when the flavin is reduced to its semiquinone state. The ox/sq potentials in the mutants Gly57Ala, Gly57Asn, and Gly57Asp are all decreased by approximately 60 mV (1.3 kcal/mol). Introduction of the beta-branched threonine side chain at position 57 has much larger effects on the conformations and potentials. The Thr57-Asp58 peptide adopts a trans O-down conformation when the flavin is oxidized; upon reduction to the semiquinone, the 57-58 peptide rotates to a trans O-up conformation resembling that found in the wild-type protein. Changes in FMN-protein interactions and in conformational equilibria in G57T combine to decrease the redox potential for the ox/sq equilibrium by 180 mV (+4.0 kcal/mol) and to increase the sq/hq potential by 80 mV (-1.7 kcal/mol). A thermodynamic scheme is introduced as a framework for rationalizing the properties of wild-type flavodoxin and the effects of the mutations.

	~~{{STRUCTURE_2fvx\| PDB=2fvx \| SCENE= }}~~		Control of oxidation-reduction potentials in flavodoxin from Clostridium beijerinckii: the role of conformation changes.,Ludwig ML, Pattridge KA, Metzger AL, Dixon MM, Eren M, Feng Y, Swenson RP Biochemistry. 1997 Feb 11;36(6):1259-80. PMID:9063874<ref>PMID:9063874</ref>

	~~===CLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: G57T REDUCED (277K)===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_9063874}}~~

	~~==About this Structure==~~
	~~[[2fvx]] is~~ a ~~1 chain structure with sequence from [http://en.wikipedia~~.~~org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann.ac.il/oca-bin~~/~~ocashort?id=2FVX OCA].~~

	==See Also==		==See Also==
	*[[Flavodoxin\|Flavodoxin]]		*[[Flavodoxin\|Flavodoxin]]
			== References ==
	==~~Reference~~==		<references/>
	<~~ref group="xtra">PMID:009063874<~~/~~ref~~><~~references group="xtra"~~/>		__TOC__
			</StructureSection>
	[[Category: Clostridium beijerinckii]]		[[Category: Clostridium beijerinckii]]
	[[Category: Dixon, M M.]]		[[Category: Dixon, M M.]]

OCA at 13:07, 20 October 2012

2012-10-20T13:07:03Z

← Older revision		Revision as of 13:07, 20 October 2012
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	==About this Structure==		==About this Structure==
	[[2fvx]] is a 1 chain structure ~~of [[Flavodoxin]]~~ with sequence from [http://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVX OCA].		[[2fvx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVX OCA].

	==See Also==		==See Also==

OCA at 10:57, 26 July 2012

2012-07-26T10:57:16Z

← Older revision		Revision as of 10:57, 26 July 2012
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	[[Image:2fvx.png\|left\|200px]]		[[Image:2fvx.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2fvx", 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_2fvx\| PDB=2fvx \| SCENE= }}		{{STRUCTURE_2fvx\| PDB=2fvx \| SCENE= }}

	===CLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: G57T REDUCED (277K)===		===CLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: G57T REDUCED (277K)===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_9063874}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 9063874 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_9063874}}		{{ABSTRACT_PUBMED_9063874}}

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	==See Also==		==See Also==
	*[[Flavodoxin]]		*[[Flavodoxin\|Flavodoxin]]

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~9063874~~</ref><references group="xtra"/>		<ref group="xtra">PMID:009063874</ref><references group="xtra"/>
	[[Category: Clostridium beijerinckii]]		[[Category: Clostridium beijerinckii]]
	[[Category: Dixon, M M.]]		[[Category: Dixon, M M.]]