2fax: Difference between revisions

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<StructureSection load='2fax' size='340' side='right'caption='[[2fax]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='2fax' size='340' side='right'caption='[[2fax]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2fax]] 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=2FAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FAX FirstGlance]. <br>
<table><tr><td colspan='2'>[[2fax]] 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=2FAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FAX 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]] 1.8&#8491;</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=2fax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fax OCA], [https://pdbe.org/2fax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fax RCSB], [https://www.ebi.ac.uk/pdbsum/2fax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fax 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=2fax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fax OCA], [https://pdbe.org/2fax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fax RCSB], [https://www.ebi.ac.uk/pdbsum/2fax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fax 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=2fax 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=2fax 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., &amp; Ludwig, M. L. (1977) J. Mol. Biol. 117, 195-225; Ludwig, M. L., &amp; 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2fax" 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]]

Latest revision as of 12:22, 14 February 2024

CLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: N137A OXIDIZED (150K)CLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: N137A OXIDIZED (150K)

Structural highlights

2fax is a 1 chain structure with sequence from Clostridium beijerinckii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FLAV_CLOBE Low-potential electron donor to a number of redox enzymes.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2fax, resolution 1.80Å

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