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1frh

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[[Image:1frh.gif|left|200px]]
 
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{{Structure
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==AZOTOBACTER VINELANDII FERREDOXIN I: ALTERATION OF INDIVIDUAL SURFACE CHARGES AND THE [4FE-4S] CLUSTER REDUCTION POTENTIAL==
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|PDB= 1frh |SIZE=350|CAPTION= <scene name='initialview01'>1frh</scene>, resolution 2.3&Aring;
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<StructureSection load='1frh' size='340' side='right'caption='[[1frh]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> and <scene name='pdbligand=F3S:FE3-S4 CLUSTER'>F3S</scene>
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<table><tr><td colspan='2'>[[1frh]] 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=1FRH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FRH FirstGlance]. <br>
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|ACTIVITY=
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</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>
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|GENE= POTENTIAL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=354 Azotobacter vinelandii])
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<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>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1frh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1frh OCA], [https://pdbe.org/1frh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1frh RCSB], [https://www.ebi.ac.uk/pdbsum/1frh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1frh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fr/1frh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1frh ConSurf].
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<div style="clear:both"></div>
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'''AZOTOBACTER VINELANDII FERREDOXIN I: ALTERATION OF INDIVIDUAL SURFACE CHARGES AND THE [4FE-4S] CLUSTER REDUCTION POTENTIAL'''
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==See Also==
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*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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==About this Structure==
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1FRH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRH OCA].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/8132582 8132582]
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[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Stout, C D.]]
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[[Category: Stout CD]]
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[[Category: F3S]]
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[[Category: SF4]]
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[[Category: electron transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:13:00 2008''
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Current revision

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

PDB ID 1frh

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