Crystal structure of the cofactor-free form of thioredoxin reductase from Acinetobacter baumannii
- Authors
- Chun, Hye Lin; Chang, Ye Ji; Park, Hyun Ho
- Issue Date
- Aug-2021
- Publisher
- WILEY
- Keywords
- Acinetobacter baumannii; crystal structure; redox homeostasis; superbugs; thioredoxin reductase
- Citation
- FEBS LETTERS, v.595, no.15, pp 1977 - 1986
- Pages
- 10
- Journal Title
- FEBS LETTERS
- Volume
- 595
- Number
- 15
- Start Page
- 1977
- End Page
- 1986
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/49298
- DOI
- 10.1002/1873-3468.14149
- ISSN
- 0014-5793
1873-3468
- Abstract
- 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 angstrom high-resolution structure of TrxR from Acinetobacter baumannii Thioredoxin reductase (AbTrxR), which is a Gram-negative, pathogenic bacterium and a drug-resistant superbug. AbTrxR was cofactor-free and formed a dimer in solution. AbTrxR contained a longer dimerization loop2 and a shorter beta(7)-beta(8) connecting loop than other TrxRs. AbTrxR 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.
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