1F6M

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

1F6M の概要

• エントリーDOI: 10.2210/pdb1f6m/pdb
• 関連するPDBエントリー: 1TDF
• 分子名称: THIOREDOXIN REDUCTASE, THIOREDOXIN 1, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: alternate conformation, ternary complex, domain motion, redox-active center, nadp, fad, electron transport, oxidoreductase
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm: P0A9P4
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 190747.91

構造登録者

Lennon, B.W.,Williams Jr., C.H.,Ludwig, M.L. (登録日: 2000-06-22, 公開日: 2000-08-30, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.95 Å)