Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry

Dorothy D. Majewski, Liam J. Worrall, Chuan Hong, Claire E. Atkinson, Marija Vuckovic, Nobuhiko Watanabe, Zhiheng Yu () and Natalie C. J. Strynadka ()
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Dorothy D. Majewski: University of British Columbia
Liam J. Worrall: University of British Columbia
Chuan Hong: Howard Hughes Medical Institute
Claire E. Atkinson: University of British Columbia
Marija Vuckovic: University of British Columbia
Nobuhiko Watanabe: University of British Columbia
Zhiheng Yu: Howard Hughes Medical Institute
Natalie C. J. Strynadka: University of British Columbia

Nature Communications, 2019, vol. 10, issue 1, 1-12

Abstract: Abstract Many Gram-negative bacteria, including causative agents of dysentery, plague, and typhoid fever, rely on a type III secretion system – a multi-membrane spanning syringe-like apparatus – for their pathogenicity. The cytosolic ATPase complex of this injectisome is proposed to play an important role in energizing secretion events and substrate recognition. We present the 3.3 Å resolution cryo-EM structure of the enteropathogenic Escherichia coli ATPase EscN in complex with its central stalk EscO. The structure shows an asymmetric pore with different functional states captured in its six catalytic sites, details directly supporting a rotary catalytic mechanism analogous to that of the heterohexameric F1/V1-ATPases despite its homohexameric nature. Situated at the C-terminal opening of the EscN pore is one molecule of EscO, with primary interaction mediated through an electrostatic interface. The EscN-EscO structure provides significant atomic insights into how the ATPase contributes to type III secretion, including torque generation and binding of chaperone/substrate complexes.

Date: 2019
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DOI: 10.1038/s41467-019-08477-7

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