1dj7: Difference between revisions

Revision as of 13:54, 2 May 2008

CRYSTAL STRUCTURE OF FERREDOXIN THIOREDOXIN REDUCTASE

OverviewOverview

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 StructureAbout this Structure

1DJ7 is a Protein complex structure of sequences from Synechocystis sp.. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Fri May 2 13:54:28 2008

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OCA

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 [[Image:1dj7.gif|left|200px]]
- {{Structure
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-}}
 '''CRYSTAL STRUCTURE OF FERREDOXIN THIOREDOXIN REDUCTASE'''
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 [[Category: Schwendtmayer, C.]]
 [[Category: 4fe-4s cluster binding fold with cxcx16cxcx8cxc binding motif]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:54:28 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:42:30 2008''