1awd: Difference between revisions
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|PDB= 1awd |SIZE=350|CAPTION= <scene name='initialview01'>1awd</scene>, resolution 1.40Å | |PDB= 1awd |SIZE=350|CAPTION= <scene name='initialview01'>1awd</scene>, resolution 1.40Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=FES:FE2/S2 (INORGANIC) CLUSTER'>FES</scene> | |LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|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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[[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]] | ||
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[[Category: metalloprotein]] | [[Category: metalloprotein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:48:50 2008'' | ||
Revision as of 18:48, 30 March 2008
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| , resolution 1.40Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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