1awd
From Proteopedia
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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: | + | [[Category: Electron transfer]] |
| - | [[Category: | + | [[Category: Electron transport]] |
| - | [[Category: | + | [[Category: Eukaryotic]] |
| - | [[Category: | + | [[Category: Green alga]] |
| - | [[Category: | + | [[Category: Metalloprotein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:46:32 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:46, 2 May 2008
FERREDOXIN [2FE-2S] OXIDIZED FORM FROM CHLORELLA FUSCA
Overview
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
1AWD is a Single protein structure of sequence from Eukaryota. Full crystallographic information is available from OCA.
Reference
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
