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• W2897765194 abstract "Abstract Eh V-ATPase is an ATP-driven Na + pump in the eubacteria Enterococcus hirae ( Eh ). Here, we present the first entire structure of detergent-solubilized Eh V-ATPase by single-particle cryo-electron microscopy (cryo-EM) using Zernike phase plate. The cryo-EM map dominantly showed one of three catalytic conformations in this rotary enzyme. To further stabilize the originally heterogeneous structure caused by the ATP hydrolysis states of the V 1 -ATPases, a peptide epitope tag system was adopted, in which the inserted peptide epitope sequence interfered with rotation of the central rotor by binding the Fab. As a result, the map unexpectedly showed another catalytic conformation of Eh V-ATPase. Interestingly, these two conformations identified with and without Fab conversely coincided with those of the minor state 2 and the major state 1 of Thermus thermophilus V/A-ATPase, respectively. The most prominent feature in Eh V-ATPase was the off-axis rotor, where the cytoplasmic V 1 domain was connected to the transmembrane V o domain through the off-axis central rotor. Furthermore, compared to the structure of ATP synthases, the larger size of the interface between the transmembrane a-subunit and c-ring of Eh V-ATPase would be more advantageous for active ion pumping." @default.
• W2897765194 created "2018-10-26" @default.
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• W2897765194 date "2018-10-23" @default.
• W2897765194 modified "2023-10-16" @default.
• W2897765194 title "Off-axis rotor in Enterococcus hirae V-ATPase visualized by Zernike phase plate single-particle cryo-electron microscopy" @default.
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• W2897765194 doi "https://doi.org/10.1038/s41598-018-33977-9" @default.
• W2897765194 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6199243" @default.
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• W2897765194 hasPublicationYear "2018" @default.
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