2pvd: Difference between revisions
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|PDB= 2pvd |SIZE=350|CAPTION= <scene name='initialview01'>2pvd</scene>, resolution 1.950Å | |PDB= 2pvd |SIZE=350|CAPTION= <scene name='initialview01'>2pvd</scene>, resolution 1.950Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |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.]) | |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.]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2pu9|2PU9]], [[2puk|2PUK]], [[2puo|2PUO]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pvd OCA], [http://www.ebi.ac.uk/pdbsum/2pvd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2pvd RCSB]</span> | |||
}} | }} | ||
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[[Category: Synechocystis sp.]] | [[Category: Synechocystis sp.]] | ||
[[Category: Dai, S.]] | [[Category: Dai, S.]] | ||
[[Category: iron-sulfur]] | [[Category: iron-sulfur]] | ||
[[Category: redox]] | [[Category: redox]] | ||
[[Category: thioredoxin]] | [[Category: thioredoxin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:41:18 2008'' | ||
Revision as of 04:41, 31 March 2008
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| , resolution 1.950Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | ftrC (Synechocystis sp.), ftrV (Synechocystis sp.) | ||||||
| Related: | 2PU9, 2PUK, 2PUO
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal srtucture of the reduced 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
2PVD 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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