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A Conserved Stable Core Structure in the Passenger Domain β-Helix of Autotransporter Virulence Proteins by Jonathan P. Renn; Patricia L. Clark is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract In Gram‐negative bacteria, a wide variety of virulence factors are secreted via the autotransporter (AT) pathway. Intriguingly, there is no significant concentration of ATP in the periplasm, nor a proton gradient across the OM, so the energetic origin of efficient secretion of AT proteins is unknown. More than 97% of AT proteins are predicted to contain right‐handed parallel β‐helical structure, and the three crystal structures available for AT passenger domains each contain a long right‐handed parallel β‐helix. Previous studies have shown that pertactin, an AT from Bordetella pertussis, exhibits three‐state folding and has a C‐terminal stable core structure. Here, we show that Pet, an unrelated AT from Escherichia coli, also exhibits three‐state unfolding and also has a stable core structure. Deletion mutants, mass spectrometry, and N‐terminal sequencing demonstrate that the Pet stable core is also located near the C‐terminus of the passenger domain. Moreover, sequence analysis suggests that three‐state folding and a C‐terminal stable core structure could be important general features of the biogenesis of AT proteins in vivo. © 2008 Wiley Periodicals, Inc. Biopolymers

Who reads A Conserved Stable Core Structure in the Passenger Domain β-Helix of Autotransporter Virulence Proteins?

Author

Jonathan P. Renn; Patricia L. Clark

Publisher

Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0006-3525)

Published

2008

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)