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TitleOff-axis rotor in Enterococcus hirae V-ATPase visualized by Zernike phase plate single-particle cryo-electron microscopy.
Journal, issue, pagesSci Rep, Vol. 8, Issue 1, Page 15632, Year 2018
Publish dateOct 23, 2018
AuthorsJun Tsunoda / Chihong Song / Fabiana Lica Imai / Junichi Takagi / Hiroshi Ueno / Takeshi Murata / Ryota Iino / Kazuyoshi Murata /
PubMed AbstractEhV-ATPase is an ATP-driven Na pump in the eubacteria Enterococcus hirae (Eh). Here, we present the first entire structure of detergent-solubilized EhV-ATPase by single-particle cryo-electron ...EhV-ATPase is an ATP-driven Na pump in the eubacteria Enterococcus hirae (Eh). Here, we present the first entire structure of detergent-solubilized EhV-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-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 EhV-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 EhV-ATPase was the off-axis rotor, where the cytoplasmic V domain was connected to the transmembrane V 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 EhV-ATPase would be more advantageous for active ion pumping.
External linksSci Rep / PubMed:30353110 / PubMed Central
MethodsEM (single particle)
Resolution17.0 - 19.0 Å
Structure data

EMDB-6977:
Enterococcus hirae V-ATPase
Method: EM (single particle) / Resolution: 17.0 Å

EMDB-6978:
EhV-ATPase with Fab at 19A resolution
Method: EM (single particle) / Resolution: 19.0 Å

EMDB-9661:
17A ZPC cryoEM map of Eh V-ATPase
Method: EM (single particle) / Resolution: 17.0 Å

EMDB-9662:
19A ZPC cryo-EM map of Eh V-ATPase-Fab
Method: EM (single particle) / Resolution: 19.0 Å

Source
  • Enterococcus hirae (bacteria)

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