1frl: Difference between revisions

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New page: left|200px<br /><applet load="1frl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1frl, resolution 2.3Å" /> '''AZOTOBACTER VINELANDI...
 
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[[Image:1frl.gif|left|200px]]<br /><applet load="1frl" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1frl, resolution 2.3&Aring;" />
'''AZOTOBACTER VINELANDII FERREDOXIN I: ALTERATION OF INDIVIDUAL SURFACE CHARGES AND THE [4FE-4S] CLUSTER REDUCTION POTENTIAL'''<br />


==Overview==
==AZOTOBACTER VINELANDII FERREDOXIN I: ALTERATION OF INDIVIDUAL SURFACE CHARGES AND THE [4FE-4S] CLUSTER REDUCTION POTENTIAL==
The structures of Azotobacter vinelandii ferredoxin I (AvFdI) and, Peptococcus aerogenes ferredoxin (PaFd), near their analogous [4e-4S]2+/+, clusters, are highly conserved (Backes, G., Mino, Y., Loehr, T.M., Meyer, T.E., Cusanovich, M.A., Sweeney, W.V., Adman, E.T., and Sanders-Loehr, J., (1991) J. Am. Chem. Soc. 11, 2055-2064). Despite these similarities, the, reduction potential (E0') of the AvFdI [4Fe-4S]2+/+ cluster is more than, 200 mV more negative than that of PaFd. We have tested the contribution, that individual amino acid residues make to the control of E0' by, converting residues in AvFdI into the corresponding residue in PaFd. Four, mutations involved substitutions of negatively charged surface residues, with neutral residues and two involved substitution of buried hydrophobic, residues. All AvFdI variants were characterized by x-ray crystallography, absorption, CD, EPR, and 1H NMR spectroscopies and by electrochemical, methods. For the F25I mutation, significant structural changes occurred, that affected the EPR and 1H NMR spectroscopic properties of AvFdI and had, a minor influence on E0'. For all other mutations there were no changes in, reduction potential. Thus we conclude, that variations in charged surface, residues do not account for the observed differences in E0' between the, analogous [4Fe-4S]2+/+ cluster of PaFd and AvFdI. These differences are, therefore most likely to be due to differences in solvent accessibility.
<StructureSection load='1frl' size='340' side='right'caption='[[1frl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1frl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FRL 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=1frl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1frl OCA], [https://pdbe.org/1frl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1frl RCSB], [https://www.ebi.ac.uk/pdbsum/1frl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1frl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FER1_AZOVI FER1_AZOVI] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. This ferredoxin could play a role in regulating gene expression by interacting directly with DNA.
== 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/fr/1frl_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=1frl ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FRL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with SF4 and F3S as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FRL OCA].
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Azotobacter vinelandii ferredoxin I. Alteration of individual surface charges and the [4FE-4S]2+/+ cluster reduction potential., Shen B, Jollie DR, Stout CD, Diller TC, Armstrong FA, Gorst CM, La Mar GN, Stephens PJ, Burgess BK, J Biol Chem. 1994 Mar 18;269(11):8564-75. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8132582 8132582]
[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Stout, C.D.]]
[[Category: Stout CD]]
[[Category: F3S]]
[[Category: SF4]]
[[Category: electron transport]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:11:57 2007''

Latest revision as of 10:18, 7 February 2024

AZOTOBACTER VINELANDII FERREDOXIN I: ALTERATION OF INDIVIDUAL SURFACE CHARGES AND THE [4FE-4S] CLUSTER REDUCTION POTENTIALAZOTOBACTER VINELANDII FERREDOXIN I: ALTERATION OF INDIVIDUAL SURFACE CHARGES AND THE [4FE-4S] CLUSTER REDUCTION POTENTIAL

Structural highlights

1frl is a 1 chain structure with sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FER1_AZOVI Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. This ferredoxin could play a role in regulating gene expression by interacting directly with DNA.

Evolutionary Conservation

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

See Also

1frl, resolution 2.30Å

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