The transiently ordered regions in intrinsically disordered ExsE are correlated with structural elements involved in chaperone binding.

ABSTRACT: Many Gram-negative bacteria utilize a type III secretion system (T3SS) to deliver protein effectors to target host cells. Transcriptional control of T3SS gene expression is generally coupled to secretion through the release of a regulatory protein. T3SS gene expression in Pseudomonas aeruginosa is regulated by extracellular secretion of ExsE. ExsE is a small 81 residue protein that appears to lack a stable structural core as indicated by previous studies. In this study, we employed various NMR methods to characterize the structure of ExsE alone and when bound to its secretion chaperone ExsC. We found that ExsE is largely unfolded throughout the polypeptide chain, belonging to a class of proteins that are intrinsically disordered. The unfolded, extended conformation of ExsE may expedite eff

SUBMITTER: Zheng Z 

PROVIDER: S-EPMC4930836 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature