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Crystal structure of the cofactor‐free form of thioredoxin reductase from Acinetobacter baumannii
Author(s) -
Chun Hye Lin,
Chang Ye Ji,
Park Hyun Ho
Publication year - 2021
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.14149
Subject(s) - thioredoxin reductase , cofactor , thioredoxin , reductase , flavin group , chemistry , biochemistry , acinetobacter baumannii , oxidoreductase , dimer , enzyme , microbiology and biotechnology , bacteria , biology , pseudomonas aeruginosa , organic chemistry , genetics
Thioredoxin reductase (TrxR) is a central component in the thioredoxin system by involving in catalyzing the reduction of thioredoxin, which is critical for organism survival. Because this system is essential, it is a promising target for novel antimicrobial agents. Herein, we solved the 1.9 Å high‐resolution structure of TrxR from Acinetobacter baumannii Thioredoxin reductase ( Ab TrxR), which is a Gram‐negative, pathogenic bacterium and a drug‐resistant superbug. Ab TrxR was cofactor‐free and formed a dimer in solution. Ab TrxR contained a longer dimerization loop2 and a shorter β 7 ‐β 8 connecting loop than other TrxRs. Ab TrxR cofactor‐free form exhibited a flavin‐oxidizing (FO) conformation, whose NADPH domain was located close to the dimeric interface. This structural information might be helpful for development of new antibiotic agents targeting superbugs.