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==S35C Flavodoxin Mutant in the semiquinone state==
==S35C Flavodoxin Mutant in the semiquinone state==
<StructureSection load='1xt6' size='340' side='right' caption='[[1xt6]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1xt6' size='340' side='right'caption='[[1xt6]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1xt6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Desvh Desvh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XT6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1xt6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_vulgaris_str._Hildenborough Desulfovibrio vulgaris str. Hildenborough]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XT6 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='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='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=1xt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xt6 OCA], [http://pdbe.org/1xt6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xt6 RCSB], [http://www.ebi.ac.uk/pdbsum/1xt6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xt6 ProSAT]</span></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=1xt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xt6 OCA], [https://pdbe.org/1xt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xt6 RCSB], [https://www.ebi.ac.uk/pdbsum/1xt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xt6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/FLAV_DESVH FLAV_DESVH]] Low-potential electron donor to a number of redox enzymes.  
[https://www.uniprot.org/uniprot/FLAV_DESVH FLAV_DESVH] 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=1xt6 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=1xt6 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystallographic structure of an engineered flavodoxin mutant from Desulfovibrio vulgaris has been analysed. Site-directed mutagenesis was used to substitute serine 35 with a cysteine to provide a possible covalent linkage. The crystal structure of the semiquinone form of this mutant is similar to the corresponding oxidation state of the wild-type flavodoxin. Analysis of the structural changes reveals the interaction between N(5)H of the flavin and the carbonyl O atom of Gly61 to be critical for modulation of the electrochemical properties of the protein.
Structure of S35C flavodoxin mutant from Desulfovibrio vulgaris in the semiquinone state.,Artali R, Marchini N, Meneghetti F, Cavazzini D, Cassetta A, Sassone C Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):481-4. Epub 2005, Mar 24. PMID:15805604<ref>PMID:15805604</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1xt6" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Flavodoxin|Flavodoxin]]
*[[Flavodoxin 3D structures|Flavodoxin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Desvh]]
[[Category: Desulfovibrio vulgaris str. Hildenborough]]
[[Category: Artali, R]]
[[Category: Large Structures]]
[[Category: Bombieri, G]]
[[Category: Artali R]]
[[Category: Cassetta, A]]
[[Category: Bombieri G]]
[[Category: Cavazzini, D]]
[[Category: Cassetta A]]
[[Category: Gilardi, G]]
[[Category: Cavazzini D]]
[[Category: Marchini, N]]
[[Category: Gilardi G]]
[[Category: Meneghetti, F]]
[[Category: Marchini N]]
[[Category: Rossi, G L]]
[[Category: Meneghetti F]]
[[Category: Sassone, C]]
[[Category: Rossi GL]]
[[Category: Electron transport]]
[[Category: Sassone C]]
[[Category: Flavodoxin]]
[[Category: Mutant]]
[[Category: Protein]]
[[Category: S35c]]

Latest revision as of 11:53, 14 February 2024

S35C Flavodoxin Mutant in the semiquinone stateS35C Flavodoxin Mutant in the semiquinone state

Structural highlights

1xt6 is a 1 chain structure with sequence from Desulfovibrio vulgaris str. Hildenborough. 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_DESVH 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

1xt6, resolution 1.80Å

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