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[[Image:1fld.gif|left|200px]]<br />
<applet load="1fld" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fld, resolution 1.8&Aring;" />
'''CLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: G57T OXIDIZED'''<br />


==Overview==
==CLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: G57T 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='1fld' size='340' side='right'caption='[[1fld]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fld]] 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=1FLD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FLD 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]] 1.8&#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=1fld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fld OCA], [https://pdbe.org/1fld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fld RCSB], [https://www.ebi.ac.uk/pdbsum/1fld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fld 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/fl/1fld_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=1fld ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FLD 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]]. Structure known Active Site: FMN. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FLD 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]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:12:27 2007''

Latest revision as of 10:15, 7 February 2024

CLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: G57T OXIDIZEDCLOSTRIDIUM BEIJERINCKII FLAVODOXIN MUTANT: G57T OXIDIZED

Structural highlights

1fld 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

1fld, resolution 1.80Å

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