7YSI

Crystal structure of thioredoxin 2

Summary for 7YSI

• Entry DOI: 10.2210/pdb7ysi/pdb
• Descriptor: Thiol disulfide reductase thioredoxin, ZINC ION (3 entities in total)
• Functional Keywords: trx2, thioredoxin2, oxidoreductase
• Biological source: Acinetobacter baumannii
• Total number of polymer chains: 1
• Total formula weight: 16867.07

Authors

Chang, Y.J.,Park, H.H. (deposition date: 2022-08-12, release date: 2023-03-15, Last modification date: 2024-10-30)

Primary citation

Chang, Y.J.,Sung, J.H.,Lee, C.S.,Lee, J.H.,Park, H.H.
Comparison of the structure and activity of thioredoxin 2 and thioredoxin 1 from Acinetobacter baumannii.
Iucrj, 10:147-155, 2023

PubMed Abstract: Thioredoxin (Trx) is essential in a redox-control system, with many bacteria containing two Trxs: Trx1 and Trx2. Due to a Trx system's critical function, Trxs are targets for novel antibiotics. Here, a 1.20 Å high-resolution structure of Trx2 from Acinetobacter baumannii (abTrx2), an antibiotic resistant pathogenic superbug, is elucidated. By comparing Trx1 and Trx2, it is revealed that the two Trxs possess similar activity, although Trx2 contains an additional N-terminal zinc-finger domain and exhibits more flexible properties in solution. Finally, it is shown that the Trx2 zinc-finger domain might be rotatable and that proper zinc coordination at the zinc-finger domain is critical to abTrx2 activity. This study enhances understanding of the Trx system and will facilitate the design of novel antibiotics.

PubMed: 36752373
DOI: 10.1107/S2052252523000404

Experimental method

X-RAY DIFFRACTION (1.202 Å)