1f6m
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CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THIOREDOXIN REDUCTASE, THIOREDOXIN, AND THE NADP+ ANALOG, AADP+
OverviewOverview
In thioredoxin reductase (TrxR) from Escherichia coli, cycles of reduction, and reoxidation of the flavin adenine dinucleotide (FAD) cofactor depend, on rate-limiting rearrangements of the FAD and NADPH (reduced form of, nicotinamide adenine dinucleotide phosphate) domains. We describe the, structure of the flavin-reducing conformation of E. coli TrxR at a, resolution of 3.0 angstroms. The orientation of the two domains permits, reduction of FAD by NADPH and oxidation of the enzyme dithiol by the, protein substrate, thioredoxin. The alternate conformation, described by, Kuriyan and co-workers, permits internal transfer of reducing equivalents, from reduced FAD to the active-site disulfide. Comparison of these, structures demonstrates that switching between the two conformations, involves a "ball-and-socket" motion in which the pyridine, nucleotide-binding domain rotates by 67 degrees.
About this StructureAbout this Structure
1F6M is a Protein complex structure of sequences from Escherichia coli with FAD and 3AA as ligands. Active as Thioredoxin-disulfide reductase, with EC number 1.8.1.9 Full crystallographic information is available from OCA.
ReferenceReference
Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase., Lennon BW, Williams CH Jr, Ludwig ML, Science. 2000 Aug 18;289(5482):1190-4. PMID:10947986
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