2pvg: Difference between revisions

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|PDB= 2pvg |SIZE=350|CAPTION= <scene name='initialview01'>2pvg</scene>, resolution 2.400&Aring;
|PDB= 2pvg |SIZE=350|CAPTION= <scene name='initialview01'>2pvg</scene>, resolution 2.400&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene> and <scene name='pdbligand=SF4:IRON/SULFUR CLUSTER'>SF4</scene>
|LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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.]), petF, fed ([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.]), petF, fed ([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]], [[2pvd|2PVD]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pvg OCA], [http://www.ebi.ac.uk/pdbsum/2pvg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2pvg RCSB]</span>
}}
}}


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[[Category: Synechocystis sp.]]
[[Category: Synechocystis sp.]]
[[Category: Dai, S.]]
[[Category: Dai, S.]]
[[Category: FES]]
[[Category: SF4]]
[[Category: ferredoxin. redox]]
[[Category: ferredoxin. redox]]
[[Category: iron-sulfur]]
[[Category: iron-sulfur]]
[[Category: thioredoxin]]
[[Category: thioredoxin]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:17:57 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:41:19 2008''

Revision as of 04:41, 31 March 2008

File:2pvg.jpg


PDB ID 2pvg

Drag the structure with the mouse to rotate
, resolution 2.400Å
Ligands: ,
Gene: ftrC (Synechocystis sp.), ftrV (Synechocystis sp.), petF, fed (Synechocystis sp.)
Related: 2PU9, 2PUK, 2PUO, 2PVD


Resources: FirstGlance, OCA, PDBsum, RCSB
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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