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New page: left|200px<br /><applet load="1qof" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qof, resolution 1.8Å" /> '''FERREDOXIN MUTATION Q...
 
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[[Image:1qof.gif|left|200px]]<br /><applet load="1qof" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1qof, resolution 1.8&Aring;" />
'''FERREDOXIN MUTATION Q70K'''<br />


==Overview==
==FERREDOXIN MUTATION Q70K==
A combination of structural, thermodynamic, and transient kinetic data on, wild-type and mutant Anabaena vegetative cell ferredoxins has been used to, investigate the nature of the protein-protein interactions leading to, electron transfer from reduced ferredoxin to oxidized ferredoxin:NADP+, reductase (FNR). We have determined the reduction potentials of wild-type, vegetative ferredoxin, heterocyst ferredoxin, and 12 site-specific mutants, at seven surface residues of vegetative ferredoxin, as well as the one-, and two-electron reduction potentials of FNR, both alone and in complexes, with wild-type and three mutant ferredoxins. X-ray crystallographic, structure determinations have been carried out for six of the ferredoxin, mutants. None of the mutants showed significant structural changes in the, immediate vicinity of the [2Fe-2S] cluster, despite large decreases in, electron-transfer reactivity (for E94K and S47A) and sizable increases in, reduction potential (80 mV for E94K and 47 mV for S47A). Furthermore, the, relatively small changes in Calpha backbone atom positions which were, observed in these mutants do not correlate with the kinetic and, thermodynamic properties. In sharp contrast to the S47A mutant, S47T, retains electron-transfer activity, and its reduction potential is 100 mV, more negative than that of the S47A mutant, implicating the importance of, the hydrogen bond which exists between the side chain hydroxyl group of, S47 and the side chain carboxyl oxygen of E94. Other ferredoxin mutations, that alter both reduction potential and electron-transfer reactivity are, E94Q, F65A, and F65I, whereas D62K, D68K, Q70K, E94D, and F65Y have, reduction potentials and electron-transfer reactivity that are similar to, those of wild-type ferredoxin. In electrostatic complexes with recombinant, FNR, three of the kinetically impaired ferredoxin mutants, as did, wild-type ferredoxin, induced large (approximately 40 mV) positive shifts, in the reduction potential of the flavoprotein, thereby making electron, transfer thermodynamically feasible. On the basis of these observations, we conclude that nonconservative mutations of three critical residues, (S47, F65, and E94) on the surface of ferredoxin have large parallel, effects on both the reduction potential and the electron-transfer, reactivity of the [2Fe-2S] cluster and that the reduction potential, changes are not the principal factor governing electron-transfer, reactivity. Rather, the kinetic properties are most likely controlled by, the specific orientations of the proteins within the transient, electron-transfer complex.
<StructureSection load='1qof' size='340' side='right'caption='[[1qof]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1qof]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QOF 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=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=1qof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qof OCA], [https://pdbe.org/1qof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qof RCSB], [https://www.ebi.ac.uk/pdbsum/1qof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qof ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FER1_NOSS1 FER1_NOSS1] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
== 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/qo/1qof_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=1qof ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1QOF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with SO4 and FES as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QOF OCA].
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structure-function relationships in Anabaena ferredoxin: correlations between X-ray crystal structures, reduction potentials, and rate constants of electron transfer to ferredoxin:NADP+ reductase for site-specific ferredoxin mutants., Hurley JK, Weber-Main AM, Stankovich MT, Benning MM, Thoden JB, Vanhooke JL, Holden HM, Chae YK, Xia B, Cheng H, Markley JL, Martinez-Julvez M, Gomez-Moreno C, Schmeits JL, Tollin G, Biochemistry. 1997 Sep 16;36(37):11100-17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9287153 9287153]
[[Category: Large Structures]]
[[Category: Anabaena sp.]]
[[Category: Nostoc sp. PCC 7120 = FACHB-418]]
[[Category: Single protein]]
[[Category: Benning MM]]
[[Category: Benning, M.M.]]
[[Category: Holden HM]]
[[Category: Holden, H.M.]]
[[Category: FES]]
[[Category: SO4]]
[[Category: electron transport]]
[[Category: ferredoxin]]
[[Category: iron-sulfur]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:50:44 2007''

Latest revision as of 11:15, 14 February 2024

FERREDOXIN MUTATION Q70KFERREDOXIN MUTATION Q70K

Structural highlights

1qof is a 2 chain structure with sequence from Nostoc sp. PCC 7120 = FACHB-418. 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

FER1_NOSS1 Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.

Evolutionary Conservation

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

See Also

1qof, resolution 1.80Å

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