1ff2: Difference between revisions

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OCA

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-[[Image:1ff2.jpg|left|200px]]<br /><applet load="1ff2" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1ff2, resolution 2.30&Aring;" />
-'''CRYSTAL STRUCTURE OF THE C42D MUTANT OF AZOTOBACTER VINELANDII 7FE FERREDOXIN (FDI)'''<br />
-==Overview==
+==CRYSTAL STRUCTURE OF THE C42D MUTANT OF AZOTOBACTER VINELANDII 7FE FERREDOXIN (FDI)==
-All naturally occurring ferredoxins that have Cys-X-X-Asp-X-X-Cys motifs, contain [4Fe-4S](2+/+) clusters that can be easily and reversibly, converted to [3Fe-4S](+/0) clusters. In contrast, ferredoxins with, unmodified Cys-X-X-Cys-X-X-Cys motifs assemble [4Fe-4S](2+/+) clusters, that cannot be easily interconverted with [3Fe-4S](+/0) clusters. In this, study we changed the central cysteine of the, Cys(39)-X-X-Cys(42)-X-X-Cys(45) of Azotobacter vinelandii FdI, which, coordinates its [4Fe-4S](2+/+) cluster, into an aspartate. UV-visible, EPR, and CD spectroscopies, metal analysis, and x-ray crystallography show, that, like native FdI, aerobically purified C42D FdI is a seven-iron, protein retaining its [4Fe-4S](2+/+) cluster with monodentate aspartate, ligation to one iron. Unlike known clusters of this type the reduced, [4Fe-4S](+) cluster of C42D FdI exhibits only an S = 1/2 EPR with no, higher spin signals detected. The cluster shows only a minor change in, reduction potential relative to the native protein. All attempts to, convert the cluster to a 3Fe cluster using conventional methods of oxygen, or ferricyanide oxidation or thiol exchange were not successful. The, cluster conversion was ultimately accomplished using a new electrochemical, method. Hydrophobic and electrostatic interaction and the lack of Gly, residues adjacent to the Asp ligand explain the remarkable stability of, this cluster.
+<StructureSection load='1ff2' size='340' side='right'caption='[[1ff2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ff2]] 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=1FF2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FF2 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]] 2.3&#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=1ff2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ff2 OCA], [https://pdbe.org/1ff2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ff2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ff2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ff2 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/ff/1ff2_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=1ff2 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-FF2 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=1FF2 OCA].
+*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Structure of C42D Azotobacter vinelandii FdI. A Cys-X-X-Asp-X-X-Cys motif ligates an air-stable [4Fe-4S]2+/+ cluster., Jung YS, Bonagura CA, Tilley GJ, Gao-Sheridan HS, Armstrong FA, Stout CD, Burgess BK, J Biol Chem. 2000 Nov 24;275(47):36974-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10961993 10961993]
 [[Category: Azotobacter vinelandii]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Burgess, B.K.]]
+[[Category: Burgess BK]]
-[[Category: Stout, C.D.]]
+[[Category: Stout CD]]
-[[Category: F3S]]
-[[Category: SF4]]
-[[Category: 7fe ferredoxin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:52:02 2007''