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New page: left|200px<br /><applet load="1awd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1awd, resolution 1.40Å" /> '''FERREDOXIN [2FE-2S] ...
 
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[[Image:1awd.gif|left|200px]]<br /><applet load="1awd" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1awd, resolution 1.40&Aring;" />
'''FERREDOXIN [2FE-2S] OXIDIZED FORM FROM CHLORELLA FUSCA'''<br />


==Overview==
==FERREDOXIN [2FE-2S] OXIDIZED FORM FROM CHLORELLA FUSCA==
BACKGROUND: [2Fe-2S] ferredoxins, also called plant-type ferredoxins, are, low-potential redox proteins that are widely distributed in biological, systems. In photosynthesis, the plant-type ferredoxins function as the, central molecule for distributing electrons from the photolysis of water, to a number of ferredox-independent enzymes, as well as to cyclic, photophosphorylation electron transfer. This paper reports only the second, structure of a [2Fe-2S] ferredoxin from a eukaryotic organism in its, native form. RESULTS: Ferredoxin from the green algae Chlorella fusca has, been purified, characterised, crystallised and its structure determined to, 1.4 A resolution - the highest resolution structure published to date for, a plant-type ferredoxin. The structure has the general features of the, plant-type ferredoxins already described, with conformational differences, corresponding to regions of higher mobility. Immunological data indicate, that a serine residue within the protein is partially phosphorylated. A, slightly electropositive shift in the measured redox potential value, -325, mV, is observed in comparison with other ferredoxins. CONCLUSIONS: This, high-resolution structure provides a detailed picture of the, hydrogen-bonding pattern around the [2Fe-2S] cluster of a plant-type, ferredoxin; for the first time, it was possible to obtain reliable error, estimates for the geometrical parameters. The presence of phosphoserine in, the protein indicates a possible mechanism for the regulation of the, distribution of reducing power from the photosynthetic electron-transfer, chain.
<StructureSection load='1awd' size='340' side='right'caption='[[1awd]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1awd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlorella_fusca Chlorella fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AWD 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]] 1.4&#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=1awd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1awd OCA], [https://pdbe.org/1awd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1awd RCSB], [https://www.ebi.ac.uk/pdbsum/1awd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1awd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FER_SCEFU FER_SCEFU]
== 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/aw/1awd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1awd ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: [2Fe-2S] ferredoxins, also called plant-type ferredoxins, are low-potential redox proteins that are widely distributed in biological systems. In photosynthesis, the plant-type ferredoxins function as the central molecule for distributing electrons from the photolysis of water to a number of ferredox-independent enzymes, as well as to cyclic photophosphorylation electron transfer. This paper reports only the second structure of a [2Fe-2S] ferredoxin from a eukaryotic organism in its native form. RESULTS: Ferredoxin from the green algae Chlorella fusca has been purified, characterised, crystallised and its structure determined to 1.4 A resolution - the highest resolution structure published to date for a plant-type ferredoxin. The structure has the general features of the plant-type ferredoxins already described, with conformational differences corresponding to regions of higher mobility. Immunological data indicate that a serine residue within the protein is partially phosphorylated. A slightly electropositive shift in the measured redox potential value, -325 mV, is observed in comparison with other ferredoxins. CONCLUSIONS: This high-resolution structure provides a detailed picture of the hydrogen-bonding pattern around the [2Fe-2S] cluster of a plant-type ferredoxin; for the first time, it was possible to obtain reliable error estimates for the geometrical parameters. The presence of phosphoserine in the protein indicates a possible mechanism for the regulation of the distribution of reducing power from the photosynthetic electron-transfer chain.


==About this Structure==
Crystal structure determination at 1.4 A resolution of ferredoxin from the green alga Chlorella fusca.,Bes MT, Parisini E, Inda LA, Saraiva LM, Peleato ML, Sheldrick GM Structure. 1999 Oct 15;7(10):1201-11. PMID:10545324<ref>PMID:10545324</ref>
1AWD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Eukaryota Eukaryota] 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=1AWD OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure determination at 1.4 A resolution of ferredoxin from the green alga Chlorella fusca., Bes MT, Parisini E, Inda LA, Saraiva LM, Peleato ML, Sheldrick GM, Structure. 1999 Oct 15;7(10):1201-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10545324 10545324]
</div>
[[Category: Eukaryota]]
<div class="pdbe-citations 1awd" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
[[Category: Sheldrick, G.M.]]
[[Category: FES]]
[[Category: electron transfer]]
[[Category: electron transport]]
[[Category: eukaryotic]]
[[Category: green alga]]
[[Category: metalloprotein]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:10:25 2007''
==See Also==
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sheldrick GM]]
Retrieved from "https://proteopedia.org/1awd"