2pvg: Difference between revisions
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[[Image:2pvg.jpg|left|200px]] | [[Image:2pvg.jpg|left|200px]] | ||
'''Crystal srtucture of the binary complex between ferredoxin and ferredoxin:thioredoxin reductase''' | {{Structure | ||
|PDB= 2pvg |SIZE=350|CAPTION= <scene name='initialview01'>2pvg</scene>, resolution 2.400Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene> and <scene name='pdbligand=SF4:IRON/SULFUR CLUSTER'>SF4</scene> | |||
|ACTIVITY= | |||
|GENE= ftrC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.]), ftrV ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.]), petF, fed ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.]) | |||
}} | |||
'''Crystal srtucture of the binary complex between ferredoxin and ferredoxin:thioredoxin reductase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2PVG is a [ | 2PVG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PVG OCA]. | ||
==Reference== | ==Reference== | ||
Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase., Dai S, Friemann R, Glauser DA, Bourquin F, Manieri W, Schurmann P, Eklund H, Nature. 2007 Jul 5;448(7149):92-6. PMID:[http:// | Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase., Dai S, Friemann R, Glauser DA, Bourquin F, Manieri W, Schurmann P, Eklund H, Nature. 2007 Jul 5;448(7149):92-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17611542 17611542] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Synechocystis sp.]] | [[Category: Synechocystis sp.]] | ||
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[[Category: thioredoxin]] | [[Category: thioredoxin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:17:57 2008'' | ||
Revision as of 19:17, 20 March 2008
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| , resolution 2.400Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | ftrC (Synechocystis sp.), ftrV (Synechocystis sp.), petF, fed (Synechocystis sp.) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal srtucture of the binary complex between ferredoxin and ferredoxin:thioredoxin reductase
OverviewOverview
Oxygen-evolving photosynthetic organisms regulate carbon metabolism through a light-dependent redox signalling pathway. Electrons are shuttled from photosystem I by means of ferredoxin (Fdx) to ferredoxin-thioredoxin reductase (FTR), which catalyses the two-electron-reduction of chloroplast thioredoxins (Trxs). These modify target enzyme activities by reduction, regulating carbon flow. FTR is unique in its use of a [4Fe-4S] cluster and a proximal disulphide bridge in the conversion of a light signal into a thiol signal. We determined the structures of FTR in both its one- and its two-electron-reduced intermediate states and of four complexes in the pathway, including the ternary Fdx-FTR-Trx complex. Here we show that, in the first complex (Fdx-FTR) of the pathway, the Fdx [2Fe-2S] cluster is positioned suitably for electron transfer to the FTR [4Fe-4S] centre. After the transfer of one electron, an intermediate is formed in which one sulphur atom of the FTR active site is free to attack a disulphide bridge in Trx and the other sulphur atom forms a fifth ligand for an iron atom in the FTR [4Fe-4S] centre--a unique structure in biology. Fdx then delivers a second electron that cleaves the FTR-Trx heterodisulphide bond, which occurs in the Fdx-FTR-Trx complex. In this structure, the redox centres of the three proteins are aligned to maximize the efficiency of electron transfer from the Fdx [2Fe-2S] cluster to the active-site disulphide of Trxs. These results provide a structural framework for understanding the mechanism of disulphide reduction by an iron-sulphur enzyme and describe previously unknown interaction networks for both Fdx and Trx (refs 4-6).
About this StructureAbout this Structure
2PVG is a Protein complex structure of sequences from Synechocystis sp.. Full crystallographic information is available from OCA.
ReferenceReference
Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase., Dai S, Friemann R, Glauser DA, Bourquin F, Manieri W, Schurmann P, Eklund H, Nature. 2007 Jul 5;448(7149):92-6. PMID:17611542
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