1awd
FERREDOXIN [2FE-2S] OXIDIZED FORM FROM CHLORELLA FUSCA
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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 with FES as ligand. 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
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