Complete fiber structures of complex trimeric autotransporter adhesins conserved in enterobacteria.

ABSTRACT: Trimeric autotransporter adhesins (TAAs) are modular, highly repetitive surface proteins that mediate adhesion to host cells in a broad range of Gram-negative pathogens. Although their sizes may differ by more than one order of magnitude, they all follow the same basic head-stalk-anchor architecture, where the head mediates adhesion and autoagglutination, the stalk projects the head from the bacterial surface, and the anchor provides the export function and attaches the adhesin to the bacterial outer membrane after export is complete. In complex adhesins, head and stalk domains may alternate several times before the anchor is reached. Despite extensive sequence divergence, the structures of TAA domains are highly constrained, due to the tight interleaving of their constituent polypeptide c

SUBMITTER: Hartmann MD 

PROVIDER: S-EPMC3529040 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature