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Publication Abstract from PubMed

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 A 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 beta-sheet surrounded by four alpha-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.

High-resolution crystal structure of Acinetobacter baumannii thioredoxin 1.,Chang YJ, Park HH Biochem Biophys Res Commun. 2022 Jun 11;608:1-7. doi: 10.1016/j.bbrc.2022.03.134. , Epub 2022 Mar 28. PMID:35378360^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.