1awd: Difference between revisions

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[[Image:1awd.gif|left|200px]]
[[Image:1awd.gif|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1awd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1awd OCA], [http://www.ebi.ac.uk/pdbsum/1awd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1awd RCSB]</span>
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'''FERREDOXIN [2FE-2S] OXIDIZED FORM FROM CHLORELLA FUSCA'''
'''FERREDOXIN [2FE-2S] OXIDIZED FORM FROM CHLORELLA FUSCA'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sheldrick, G M.]]
[[Category: Sheldrick, G M.]]
[[Category: electron transfer]]
[[Category: Electron transfer]]
[[Category: electron transport]]
[[Category: Electron transport]]
[[Category: eukaryotic]]
[[Category: Eukaryotic]]
[[Category: green alga]]
[[Category: Green alga]]
[[Category: metalloprotein]]
[[Category: Metalloprotein]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:48:50 2008''

Revision as of 10:46, 2 May 2008

File:1awd.gif

Template:STRUCTURE 1awd

FERREDOXIN [2FE-2S] OXIDIZED FORM FROM CHLORELLA FUSCA


OverviewOverview

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 StructureAbout this Structure

1AWD is a Single protein structure of sequence from Eukaryota. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Fri May 2 10:46:32 2008

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