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New page: left|200px<br /><applet load="2fd2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fd2, resolution 1.9Å" /> '''CRYSTALLOGRAPHIC ANAL...
 
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[[Image:2fd2.jpg|left|200px]]<br /><applet load="2fd2" size="450" color="white" frame="true" align="right" spinBox="true"
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'''CRYSTALLOGRAPHIC ANALYSIS OF TWO SITE-DIRECTED MUTANTS OF AZOTOBACTER VINELANDII FERREDOXIN'''<br />


==Overview==
==CRYSTALLOGRAPHIC ANALYSIS OF TWO SITE-DIRECTED MUTANTS OF AZOTOBACTER VINELANDII FERREDOXIN==
The crystal structure of the C24A mutant of Azotobacter vinelandii 7Fe, ferredoxin (FdI) has been solved and refined at 2.0-A resolution. The, structure is isomorphous to native FdI except at the site of mutation, where A24 moves toward the [4Fe-4S] cluster. In spite of this inefficient, packing results: three of five van der Waals contacts from the S gamma of, C24 in native FdI are lost and the remaining two become longer., Consequently, the [4Fe-4S] cluster is either disordered or has a higher, temperature factor (B factor) compared to the rest of the C24A FdI, molecule. In addition, the entire C24A FdI structure has a higher overall, B factor than native FdI. Therefore, in comparison to native FdI, the C24A, mutant is isomorphous but exhibits large differences in B factor, especially at the [4Fe-4S] cluster. In contrast, the C20A FdI structure, (Martin, A. G., Burgess, B. K., Stout, C. D., Cash, V. L., Dean, D. R., Jensen, G. M., and Stephens, P. J. (1990) Proc. Natl. Acad. Sci. U. S. A., 87, 598-602), which contains large structural rearrangements in the, vicinity of the [4Fe-4S] cluster, exhibits essentially no change in B, factor. The conformational change observed at residue 24 is similar in, both C24A and C20A FdI structures. The solvent accessibility of the Fe, atoms in the [3Fe-4S] and [4Fe-4S] clusters is similar in C24A, C20A, and, native FdI.
<StructureSection load='2fd2' size='340' side='right'caption='[[2fd2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2fd2]] 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=2FD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FD2 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=2fd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fd2 OCA], [https://pdbe.org/2fd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fd2 RCSB], [https://www.ebi.ac.uk/pdbsum/2fd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fd2 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/2fd2_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=2fd2 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2FD2 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=2FD2 OCA].
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystallographic analysis of two site-directed mutants of Azotobacter vinelandii ferredoxin., Soman J, Iismaa S, Stout CD, J Biol Chem. 1991 Nov 15;266(32):21558-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1939185 1939185]
[[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 Wed Nov 21 10:29:13 2007''

Latest revision as of 12:22, 14 February 2024

CRYSTALLOGRAPHIC ANALYSIS OF TWO SITE-DIRECTED MUTANTS OF AZOTOBACTER VINELANDII FERREDOXINCRYSTALLOGRAPHIC ANALYSIS OF TWO SITE-DIRECTED MUTANTS OF AZOTOBACTER VINELANDII FERREDOXIN

Structural highlights

2fd2 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

2fd2, resolution 1.90Å

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