1awd
From Proteopedia
(New page: 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=" | + | [[Image:1awd.gif|left|200px]]<br /><applet load="1awd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1awd, resolution 1.40Å" /> | caption="1awd, resolution 1.40Å" /> | ||
'''FERREDOXIN [2FE-2S] OXIDIZED FORM FROM CHLORELLA FUSCA'''<br /> | '''FERREDOXIN [2FE-2S] OXIDIZED FORM FROM CHLORELLA FUSCA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: [2Fe-2S] ferredoxins, also called plant-type ferredoxins, are | + | 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== | ==About this Structure== | ||
| - | 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:// | + | 1AWD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Eukaryota Eukaryota] with <scene name='pdbligand=FES:'>FES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AWD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Eukaryota]] | [[Category: Eukaryota]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Sheldrick, G | + | [[Category: Sheldrick, G M.]] |
[[Category: FES]] | [[Category: FES]] | ||
[[Category: electron transfer]] | [[Category: electron transfer]] | ||
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[[Category: metalloprotein]] | [[Category: metalloprotein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:58 2008'' |
Revision as of 09:48, 21 February 2008
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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 with as ligand. 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
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