High-resolution crystal structure of Acinetobacter baumannii thioredoxin 1
- Authors
- Chang, Y.J.; Park, H.H.
- Issue Date
- Jun-2022
- Publisher
- Elsevier B.V.
- Keywords
- Acinetobacter baumannii; Crystal structure; Redox homeostasis; Superbugs; Thioredoxin
- Citation
- Biochemical and Biophysical Research Communications, v.608, pp 1 - 7
- Pages
- 7
- Journal Title
- Biochemical and Biophysical Research Communications
- Volume
- 608
- Start Page
- 1
- End Page
- 7
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/57724
- DOI
- 10.1016/j.bbrc.2022.03.134
- ISSN
- 0006-291X
1090-2104
- Abstract
- Thioredoxin (Trx) is a central component of the redox control system that maintains the redox homeostasis critical for organism survival. Owing to its central role in survival, Trx is a prospective target for novel antimicrobial agents. Herein, we report a 1.45 Å high-resolution structure of Trx1 of Acinetobacter baumannii (abTrx1), an antibiotic-resistant pathogenic superbug. Although abTrx1 exhibited the canonical Trx fold, which consists of a four-stranded β-sheet surrounded by four α-helices, structural differences were detected in the loop forming the C-X-X-C redox center and the C-terminal. The unique CAPC sequence of the C-X-X-C motif in the abTrx1 redox center was characterized by mutagenesis. This study contributes to the field of drug designing against superbugs. © 2022 Elsevier Inc.
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