1F6M

CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THIOREDOXIN REDUCTASE, THIOREDOXIN, AND THE NADP+ ANALOG, AADP+

Summary for 1F6M

• Entry DOI: 10.2210/pdb1f6m/pdb
• Related: 1TDF
• Descriptor: THIOREDOXIN REDUCTASE, THIOREDOXIN 1, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: alternate conformation, ternary complex, domain motion, redox-active center, nadp, fad, electron transport, oxidoreductase
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P0A9P4
• Total number of polymer chains: 8
• Total formula weight: 190747.91

Authors

Lennon, B.W.,Williams Jr., C.H.,Ludwig, M.L. (deposition date: 2000-06-22, release date: 2000-08-30, Last modification date: 2024-11-06)

Primary citation

Lennon, B.W.,Williams Jr., C.H.,Ludwig, M.L.
Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase.
Science, 289:1190-1194, 2000

PubMed Abstract: 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.

PubMed: 10947986
DOI: 10.1126/science.289.5482.1190

Experimental method

X-RAY DIFFRACTION (2.95 Å)