Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins.

ABSTRACT: Many virulence factors secreted from pathogenic Gram-negative bacteria are autotransporter proteins. The final step of autotransporter secretion is C --> N-terminal threading of the passenger domain through the outer membrane (OM), mediated by a cotranslated C-terminal porin domain. The native structure is formed only after this final secretion step, which requires neither ATP nor a proton gradient. Sequence analysis reveals that, despite size, sequence, and functional diversity among autotransporter passenger domains, >97% are predicted to form parallel beta-helices, indicating this structural topology may be important for secretion. We report the folding behavior of pertactin, an autotransporter passenger domain from Bordetella pertussis. The pertactin beta-helix folds reversibly in isol

SUBMITTER: Junker M 

PROVIDER: S-EPMC1458770 | biostudies-literature | 2006 Mar

REPOSITORIES: biostudies-literature