The structure of Acinetobacter-secreted protease CpaA complexed with its chaperone CpaB reveals a novel mode of a T2SS chaperone–substrate interaction

Authors

Darya V. Urusova, Washington University School of Medicine in St. Louis
Rachel L. Kinsella, Washington University School of Medicine in St. Louis
Nichole D. Salinas, National Institutes of Health, Bethesda
M. Florencia Haurat, Washington University School of Medicine in St. Louis
Mario F. Feldman, Washington University School of Medicine in St. Louis
Niraj H. Tolia, Washington University School of Medicine in St. Louis

Journal

Journal of Biological Chemistry

Publication Date

2019

Volume

294

Issue

36

First Page

13344

Last Page

13354

Document Type

Open Access Publication

DOI

10.1074/jbc.RA119.009805

Rights and Permissions

This research was originally published in Journal of Biological Chemistry. Urusova, D. V., Kinsella, R. L., Salinas, N. D., Haurat, M. F., Feldman, M. F., & Tolia, N. H. (2019). The structure of acinetobacter-secreted protease CpaA complexed with its chaperone CpaB reveals a novel mode of a T2SS chaperone-substrate interaction. Journal of Biological Chemistry, 294(36), 13344-13354. doi:10.1074/jbc.RA119.009805 © the American Society for Biochemistry and Molecular Biology.

Recommended Citation

Urusova, Darya V.; Kinsella, Rachel L.; Salinas, Nichole D.; Haurat, M. Florencia; Feldman, Mario F.; and Tolia, Niraj H., "The structure of Acinetobacter-secreted protease CpaA complexed with its chaperone CpaB reveals a novel mode of a T2SS chaperone–substrate interaction." Journal of Biological Chemistry. 294, 36. 13344 - 13354. (2019).
https://digitalcommons.wustl.edu/open_access_pubs/8495