1dj7
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(New page: 200px<br /><applet load="1dj7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dj7, resolution 1.6Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 11:12, 20 November 2007
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CRYSTAL STRUCTURE OF FERREDOXIN THIOREDOXIN REDUCTASE
Overview
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.
About this Structure
1DJ7 is a Protein complex structure of sequences from Synechocystis sp. with SO4 and SF4 as ligands. Full crystallographic information is available from OCA.
Reference
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
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