1fxi

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STRUCTURE OF THE [2FE-2S] FERREDOXIN I FROM THE BLUE-GREEN ALGA APHANOTHECE SACRUM AT 2.2 ANGSTROMS RESOLUTION

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Categories: Aphanothece sacrum | Large Structures | Tsukihara T

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-[[Image:1fxi.gif|left|200px]]<br /><applet load="1fxi" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1fxi, resolution 2.2&Aring;" />
-'''STRUCTURE OF THE [2FE-2S] FERREDOXIN I FROM THE BLUE-GREEN ALGA APHANOTHECE SACRUM AT 2.2 ANGSTROMS RESOLUTION'''<br />
-==Overview==
+==STRUCTURE OF THE [2FE-2S] FERREDOXIN I FROM THE BLUE-GREEN ALGA APHANOTHECE SACRUM AT 2.2 ANGSTROMS RESOLUTION==
-Crystals of a [2Fe-2S] ferredoxin (Fd) I with a relative molecular mass of, 10,480 were obtained from the blue-green alga Aphanothece sacrum. Each, asymmetric unit of the crystal contains four molecules. An electron, density map calculated by the single isomorphous replacement method with, the anomalous dispersion at 2.5 A resolution was refined by averaging the, four molecules in the asymmetric unit. Positional and isotropic thermal, parameters for the non-hydrogen atoms of the four molecules and 158 water, molecules were refined to an R-factor (R = sigma[Fo-Fc[/sigma Fo) of 0.23, by the restrained least-squares method. The estimated root-mean-square, (r.m.s.) error for the atomic positions is 0.3 A. The r.m.s. deviations of, equivalent C alpha atoms of the asymmetric-unit molecules superposed by, the least-squares method average 0.35 A. The Fd molecule has a structure, like the beta-barrel in the molecule of the [2Fe-2S] Fd from Spirulina, platensis. A [2Fe-2S] cluster is bonded covalently to the protein molecule, by four Fe-S, in which three of the Fe-S bonds are in a loop segment from, position 38 to 47. The hydrophobic core inside the beta-barrel is formed, by seven conservative residues: Val15, Val18, Ile24, Leu51, Ile74, Ala79, and Ile87. The molecular surface around Tyr23, Tyr80 and the active center, may interact with ferredoxin-NADP+ reductase. One of the two iron atoms of, the [2Fe-2S] cluster should be more easily reduced than the other because, of differences in the hydrogen-bonding scheme and the hydrophobicity, around the atoms.
+<StructureSection load='1fxi' size='340' side='right'caption='[[1fxi]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1fxi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aphanothece_sacrum Aphanothece sacrum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FXI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FXI 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]] 2.2&#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></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=1fxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fxi OCA], [https://pdbe.org/1fxi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fxi RCSB], [https://www.ebi.ac.uk/pdbsum/1fxi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fxi ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FER_APHSA FER_APHSA] 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/fx/1fxi_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=1fxi ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-FXI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aphanothece_sacrum Aphanothece sacrum] with FES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FXI OCA].
+*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Structure of the [2Fe-2S] ferredoxin I from the blue-green alga Aphanothece sacrum at 2.2 A resolution., Tsukihara T, Fukuyama K, Mizushima M, Harioka T, Kusunoki M, Katsube Y, Hase T, Matsubara H, J Mol Biol. 1990 Nov 20;216(2):399-410. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2123937 2123937]
 [[Category: Aphanothece sacrum]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Tsukihara, T.]]
+[[Category: Tsukihara T]]
-[[Category: FES]]
-[[Category: electron transfer (iron-sulfur protein)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:26:12 2007''

1fxi

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STRUCTURE OF THE [2FE-2S] FERREDOXIN I FROM THE BLUE-GREEN ALGA APHANOTHECE SACRUM AT 2.2 ANGSTROMS RESOLUTION

Structural highlights

Function

Evolutionary Conservation

See Also

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