6njp | pdb_00006njp

Structure of the assembled ATPase EscN in complex with its central stalk EscO from the enteropathogenic E. coli (EPEC) type III secretion system

Loading... Status: waiting for Mol* initialization Structural highlights 6njp is a 7 chain structure with sequence from Escherichia coli O127:H6 str. E2348/69. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.29Å Ligands: ADP, AF3, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B7UMA5_ECO27 Publication Abstract from PubMed 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 A 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. Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry.,Majewski DD, Worrall LJ, Hong C, Atkinson CE, Vuckovic M, Watanabe N, Yu Z, Strynadka NCJ Nat Commun. 2019 Feb 7;10(1):626. doi: 10.1038/s41467-019-08477-7. PMID:30733444 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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