Evidence for alternative quaternary structure in a bacterial Type III secretion system chaperone.

ABSTRACT:

Background

Type III secretion systems are a common virulence mechanism in many Gram-negative bacterial pathogens. These systems use a nanomachine resembling a molecular needle and syringe to provide an energized conduit for the translocation of effector proteins from the bacterial cytoplasm to the host cell cytoplasm for the benefit of the pathogen. Prior to translocation specialized chaperones maintain proper effector protein conformation. The class II chaperone, Invasion plasmid gene (Ipg) C, stabilizes two pore forming translocator proteins. IpgC exists as a functional dimer to facilitate the mutually exclusive binding of both translocators.

Results

In this study, we present the 3.3 A crystal structure of an amino-terminally truncated form (residues 10-155, denoted IpgC10

SUBMITTER: Barta ML 

PROVIDER: S-EPMC2912912 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature