Class IA type III secretion system chaperone protein, similar to Escherichia coli CesT
This family includes type III secretion system (T3SS) chaperone proteins similar to Escherichia coli CesT and also contains Stm2138, a novel virulence chaperone in Salmonella enterica subsp. enterica serovar Typhimurium. In E. coli, the T3SS allows injection of the effector Tir (translocated intimin receptor), which plays a key role in enterohemorrhagic Escherichia coli (EHEC) infection, attaching and effacing (A/E) lesions, and intracellular signal transduction. CesT binds to Tir, which interacts with intimin and anchors the infected cell membrane inside the host cytoplasm for signaling.
Comment:Shows domain swap in CesT, which may either provide an alternative dimerization pattern to facilitate interaction with its target effector protein, Tir, or it may be a crystallographic artifact. Likely, in absence of domain-swap event, CesT may form dimers similar to other chaperones such as SigE
Structure:1K3E: Escherichia coli type III secretion chaperone CesT homodimer; contacts at 4.0A