1fvx: Difference between revisions

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New page: left|200px<br /> <applet load="1fvx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fvx, resolution 1.9Å" /> '''CLOSTRIDIUM BEIJERIN...
 
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[[Image:1fvx.gif|left|200px]]<br />
<applet load="1fvx" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fvx, resolution 1.9&Aring;" />
'''CLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: G57N OXIDIZED'''<br />


==Overview==
==CLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: G57N OXIDIZED==
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., ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9063874 (full description)]]
<StructureSection load='1fvx' size='340' side='right'caption='[[1fvx]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fvx]] 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=1FVX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FVX 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]] 1.9&#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=1fvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fvx OCA], [https://pdbe.org/1fvx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fvx RCSB], [https://www.ebi.ac.uk/pdbsum/1fvx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fvx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FLAV_CLOBE FLAV_CLOBE] 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/fv/1fvx_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=1fvx ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FVX is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]] with FMN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FVX OCA]].
*[[Flavodoxin 3D structures|Flavodoxin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9063874 9063874]
[[Category: Clostridium beijerinckii]]
[[Category: Clostridium beijerinckii]]
[[Category: Single protein]]
[[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: FMN]]
[[Category: electron transport]]
[[Category: flavoprotein]]
[[Category: fmn]]
 
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Latest revision as of 07:19, 7 February 2024

CLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: G57N OXIDIZED

1fvx, resolution 1.90Å

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