1DJ7

CRYSTAL STRUCTURE OF FERREDOXIN THIOREDOXIN REDUCTASE

Summary for 1DJ7

• Entry DOI: 10.2210/pdb1dj7/pdb
• Descriptor: FERREDOXIN THIOREDOXIN REDUCTASE: CATALYTIC CHAIN, FERREDOXIN THIOREDOXIN REDUCTASE: VARIABLE CHAIN, IRON/SULFUR CLUSTER, ... (5 entities in total)
• Functional Keywords: 4fe-4s cluster binding fold with cxcx16cxcx8cxc binding motif, electron transport
• Biological source: Synechocystis sp.; More
• Total number of polymer chains: 2
• Total formula weight: 22293.42

Authors

Dai, S.,Schwendtmayer, C.,Schurmann, P.,Ramaswamy, S.,Eklund, H. (deposition date: 1999-12-02, release date: 2000-02-14, Last modification date: 2017-10-11)

Primary citation

Dai, S.,Schwendtmayer, C.,Schurmann, P.,Ramaswamy, S.,Eklund, H.
Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster.
Science, 287:655-658, 2000

PubMed Abstract: 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.

PubMed: 10649999
DOI: 10.1126/science.287.5453.655

Experimental method

X-RAY DIFFRACTION (1.6 Å)