1dj7 | pdb_00001dj7

CRYSTAL STRUCTURE OF FERREDOXIN THIOREDOXIN REDUCTASE

spinqualitylabelsall models 1dj7, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1dj7 is a 2 chain structure with sequence from Aphanocapsa sp. (strain n-1). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SF4, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [Q55389_SYNY3] FTR is a [4Fe-4S] protein playing a central role in the ferredoxin/thioredoxin regulatory chain. It converts an electron signal (photoreduced ferredoxin) to a thiol signal (reduced thioredoxin) in the regulation of enzymes by reduction of specific disulfide groups. Catalyzes the light-dependent activation of several photosynthetic enzymes (By similarity).[PIRNR:PIRNR000260] [FTRV_SYNY3] FTR is a [4Fe-4S] protein playing a central role in the ferredoxin/thioredoxin regulatory chain. It converts an electron signal (photoreduced ferredoxin) to a thiol signal (reduced thioredoxin) in the regulation of enzymes by reduction of specific disulfide groups. Catalyzes the light-dependent activation of several photosynthetic enzymes (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Light generates reducing equivalents in chloroplasts that are used not only for carbon reduction, but also for the regulation of the activity of chloroplast enzymes by reduction of regulatory disulfides via the ferredoxin:thioredoxin reductase (FTR) system. FTR, the key electron/thiol transducer enzyme in this pathway, is unique in that it can reduce disulfides by an iron-sulfur cluster, a property that is explained by the tight contact of its active-site disulfide and the iron-sulfur center. The thin, flat FTR molecule makes the two-electron reduction possible by forming on one side a mixed disulfide with thioredoxin and by providing on the opposite side access to ferredoxin for delivering electrons. Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster.,Dai S, Schwendtmayer C, Schurmann P, Ramaswamy S, Eklund H Science. 2000 Jan 28;287(5453):655-8. PMID:10649999 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ferredoxin thioredoxin reductase

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