1frx

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(New page: 200px<br /><applet load="1frx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1frx, resolution 2.5&Aring;" /> '''STRUCTURE AND PROPERT...)
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[[Image:1frx.gif|left|200px]]<br /><applet load="1frx" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1frx, resolution 2.5&Aring;" />
 
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'''STRUCTURE AND PROPERTIES OF C20S FDI MUTANT'''<br />
 
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==Overview==
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==STRUCTURE AND PROPERTIES OF C20S FDI MUTANT==
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The [4Fe-4S] cluster of Azotobacter vinelandii ferredoxin I receives three, of its four ligands from a Cys-Xaa-Xaa-Cys-Xaa-Xaa-Cys sequence at, positions 39-45 while the fourth ligand, Cys20, is provided by a distal, portion of the sequence. Previously we reported that the site-directed, mutation of Cys20 to Ala (C20A protein) resulted in the formation of a new, [4Fe-4S] cluster that obtained its fourth ligand from Cys24, a free, cysteine in the native structure. That ligand exchange required, significant protein rearrangement. Here we report the conversion of Cys20, to Ser (C20S protein), which gives the protein the opportunity either to, retain the native structure and use the Ser20 O gamma as a ligand or to, rearrange and use Cys24. X-ray crystallography demonstrates that the, cluster does not use the Ser20 O gamma as a ligand; rather it rearranges, to use Cys24. In the C20S protein the [4Fe-4S] cluster has altered, stability and redox properties relative to either C20A or the native, protein.
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<StructureSection load='1frx' size='340' side='right'caption='[[1frx]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1frx]] 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=1FRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FRX FirstGlance]. <br>
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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]] 2.5&#8491;</td></tr>
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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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1frx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1frx OCA], [https://pdbe.org/1frx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1frx RCSB], [https://www.ebi.ac.uk/pdbsum/1frx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1frx 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/1frx_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=1frx ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1FRX 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=1FRX OCA].
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*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: cysteine ligation of the [4Fe-4S] cluster with protein rearrangement is preferred over serine ligation., Shen B, Jollie DR, Diller TC, Stout CD, Stephens PJ, Burgess BK, Proc Natl Acad Sci U S A. 1995 Oct 24;92(22):10064-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7479727 7479727]
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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://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:12:50 2007''
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Current revision

STRUCTURE AND PROPERTIES OF C20S FDI MUTANT

PDB ID 1frx

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