Chaperone activation and client binding of a 2-cysteine peroxiredoxin
oleh: Filipa Teixeira, Eric Tse, Helena Castro, Karl A. T. Makepeace, Ben A. Meinen, Christoph H. Borchers, Leslie B. Poole, James C. Bardwell, Ana M. Tomás, Daniel R. Southworth, Ursula Jakob
| Format: | Article |
|---|---|
| Diterbitkan: | Nature Portfolio 2019-02-01 |
Deskripsi
Many 2-Cystein Peroxiredoxins (Prx) can either function as peroxidases or chaperones when exposed to stress. Here the authors present the structures of Leishmania infantum mitochondrial Prx alone and with a bound model client protein, use crosslinking to reveal interaction regions that stabilize the bound client, and provide insights into the mechanism by which Prx’s adopt chaperone activity.