The type III bacterial chaperones protect the harmful proteins produced by pathogenic bacteria until they are delivered across membranes into the host cell. In October 29 on line Nature Structural Biology, Yu Luo and colleagues from University of British Columbia, Canada report the structures of three type III chaperones, providing important details about the function of the proteins and the mechanisms employed to modulate the virulence of invasive bacteria.

Luo et al. reported the crystal structures of two type III chaperones, one from a strain of Escherichia coli that causes intestinal bleeding, and the other from a strain of Salmonella. The structures reveal a common overall fold and formation of homodimers with variable, delocalized hydrophobic surfaces that are responsible for specific binding to a particular effector protein (Nature Structural Biology 2001, DOI: 10.1038/nsb717).

These results could lead to the development of new antibacterial drugs that...

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