1fd2: Difference between revisions

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New page: left|200px<br /><applet load="1fd2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fd2, resolution 1.9Å" /> '''SITE-DIRECTED MUTAGEN...
 
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[[Image:1fd2.gif|left|200px]]<br /><applet load="1fd2" size="450" color="white" frame="true" align="right" spinBox="true"
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'''SITE-DIRECTED MUTAGENESIS OF AZOTOBACTER VINELANDII FERREDOXIN I. (FE-S) CLUSTER-DRIVEN PROTEIN REARRANGEMENT'''<br />


==Overview==
==SITE-DIRECTED MUTAGENESIS OF AZOTOBACTER VINELANDII FERREDOXIN I. (FE-S) CLUSTER-DRIVEN PROTEIN REARRANGEMENT==
Azotobacter vinelandii ferredoxin I is a small protein that contains one, [4Fe-4S] cluster and one [3Fe-4S] cluster. Recently the x-ray crystal, structure has been redetermined and the fdxA gene, which encodes the, protein, has been cloned and sequenced. Here we report the site-directed, mutation of Cys-20, which is a ligand of the [4Fe-4S] cluster in the, native protein, to alanine and the characterization of the protein product, by x-ray crystallographic and spectroscopic methods. The data show that, the mutant protein again contains one [4Fe-4S] cluster and one [3Fe-4S], cluster. The new [4Fe-4S] cluster obtains its fourth ligand from Cys-24, a, free cysteine in the native structure. The formation of this [4Fe-4S], cluster drives rearrangement of the protein structure.
<StructureSection load='1fd2' size='340' side='right'caption='[[1fd2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fd2]] 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=1FD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FD2 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]] 1.9&#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=1fd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fd2 OCA], [https://pdbe.org/1fd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fd2 RCSB], [https://www.ebi.ac.uk/pdbsum/1fd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fd2 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/fd/1fd2_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=1fd2 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FD2 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=1FD2 OCA].
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: [Fe-S] cluster-driven protein rearrangement., Martin AE, Burgess BK, Stout CD, Cash VL, Dean DR, Jensen GM, Stephens PJ, Proc Natl Acad Sci U S A. 1990 Jan;87(2):598-602. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2153958 2153958]
[[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 transfer(iron-sulfur protein)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:49:44 2007''

Latest revision as of 10:13, 7 February 2024

SITE-DIRECTED MUTAGENESIS OF AZOTOBACTER VINELANDII FERREDOXIN I. (FE-S) CLUSTER-DRIVEN PROTEIN REARRANGEMENTSITE-DIRECTED MUTAGENESIS OF AZOTOBACTER VINELANDII FERREDOXIN I. (FE-S) CLUSTER-DRIVEN PROTEIN REARRANGEMENT

Structural highlights

1fd2 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 1.9Å
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

1fd2, resolution 1.90Å

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