1akv: Difference between revisions

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[[Image:1akv.gif|left|200px]]<br />
<applet load="1akv" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1akv, resolution 2.0&Aring;" />
'''D95A SEMIQUINONE FLAVODOXIN MUTANT FROM D. VULGARIS'''<br />


==Overview==
==D95A SEMIQUINONE FLAVODOXIN MUTANT FROM D. VULGARIS==
The side chain of aspartate 95 in flavodoxin from Desulfovibrio vulgaris, provides the closest negative charge to N(1) of the bound FMN in the, protein. Site-directed mutagenesis was used to substitute alanine, asparagine, or glutamate for this amino acid to assess the effect of this, charge on the semiquinone/hydroquinone redox potential (E(1)) of the FMN, cofactor. The D95A mutation shifts the E(1) redox potential positively by, 16 mV, while a negative shift of 23 mV occurs in the oxidized/semiquinone, midpoint redox potential (E(2)). The crystal structures of the oxidized, and semiquinone forms of this mutant are similar to the corresponding, states of the wild-type protein. In contrast to the wild-type protein, a, further change in structure occurs in the D95A mutant in the ... [[http://ispc.weizmann.ac.il/pmbin/getpm?12206666 (full description)]]
<StructureSection load='1akv' size='340' side='right'caption='[[1akv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1akv]] 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=1AKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AKV FirstGlance]. <br>
</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&#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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1akv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1akv OCA], [https://pdbe.org/1akv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1akv RCSB], [https://www.ebi.ac.uk/pdbsum/1akv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1akv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FLAV_DESVH FLAV_DESVH] Low-potential electron donor to a number of redox enzymes.
== 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/ak/1akv_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/main_output.php?pdb_ID=1akv ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1AKV is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris]] with SO4 and FMN as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: FMN. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AKV OCA]].
*[[Flavodoxin 3D structures|Flavodoxin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystallographic investigation of the role of aspartate 95 in the modulation of the redox potentials of Desulfovibrio vulgaris flavodoxin., McCarthy AA, Walsh MA, Verma CS, O'Connell DP, Reinhold M, Yalloway GN, D'Arcy D, Higgins TM, Voordouw G, Mayhew SG, Biochemistry. 2002 Sep 10;41(36):10950-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12206666 12206666]
[[Category: Desulfovibrio vulgaris str. Hildenborough]]
[[Category: Desulfovibrio vulgaris]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Higgins T]]
[[Category: Higgins, T.]]
[[Category: Mccarthy A]]
[[Category: Mccarthy, A.]]
[[Category: Walsh M]]
[[Category: Walsh, M.]]
[[Category: FMN]]
[[Category: SO4]]
[[Category: electron transfer]]
[[Category: electron transport]]
[[Category: flavodoxin]]
[[Category: flavoprotein]]
[[Category: fmn]]
[[Category: mutant]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:33:38 2007''

Latest revision as of 09:31, 7 February 2024

D95A SEMIQUINONE FLAVODOXIN MUTANT FROM D. VULGARISD95A SEMIQUINONE FLAVODOXIN MUTANT FROM D. VULGARIS

Structural highlights

1akv 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 2Å
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

1akv, resolution 2.00Å

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