6NJO

Structure of the assembled ATPase EscN from the enteropathogenic E. coli (EPEC) type III secretion system

Summary for 6NJO

• Entry DOI: 10.2210/pdb6njo/pdb
• EMDB information: 9390 9391
• Descriptor: Translocator EscN, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: atpase, type iii secretion system, adp, hexamer, hydrolase
• Biological source: Escherichia coli O127:H6 (strain E2348/69 / EPEC)
• Total number of polymer chains: 6
• Total formula weight: 297321.33

Authors

Majewski, D.D.,Worrall, L.J.,Hong, C.,Atkinson, C.E.,Vuckovic, M.,Watanabe, N.,Yu, Z.,Strynadka, N.C.J. (deposition date: 2019-01-03, release date: 2019-02-20, Last modification date: 2024-03-20)

Primary citation

Majewski, D.D.,Worrall, L.J.,Hong, C.,Atkinson, C.E.,Vuckovic, M.,Watanabe, N.,Yu, Z.,Strynadka, N.C.J.
Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry.
Nat Commun, 10:626-626, 2019

PubMed 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 F/V-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.

PubMed: 30733444
DOI: 10.1038/s41467-019-08477-7

Experimental method

ELECTRON MICROSCOPY (3.34 Å)