A type II β-turn in the Escherichia coli protein EscU undergoes auto-cleavage via a mechanism involving cyclization of a conserved asparagine residue. Structural and in vivo analysis of point and deletion mutations illustrates the subtle conformational effects of auto-cleavage in modulating the molecular features of a highly conserved surface region of EscU, a potential point of interaction with other T3SS components at the inner membrane.
- Raz Zarivach
- Wanyin Deng
- Natalie C. J. Strynadka