Conformation of the EPEC Tir protein in solution: investigating the impact of serine phosphorylation at positions 434/463.

ABSTRACT: The translocated intimin receptor (Tir) is a key virulence factor of enteropathogenic Escherichia coli and related bacteria. During infection, Tir is translocated via a type III secretion system into host intestinal epithelial cells, where it inserts into the target cell membrane and acts as a receptor for the bacterial adhesin intimin. The effects of phosphorylation by cAMP-dependent kinase at two serine residues (Ser-434 and Ser-463) within the C-terminal domain of Tir, which may be involved in mediating structural/electrostatic changes in the protein to promote membrane insertion or intermolecular interactions, have previously been investigated. This study has focused on defining the conformation of Tir in solution and assessing any conformational changes associated with serine phosphor

SUBMITTER: Race PR 

PROVIDER: S-EPMC1896257 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature