Cryo-EM structures of intact V-ATPase from bovine brain

Rong Wang; Tao Long; Abdirahman Hassan; Jin Wang; Yingyuan Sun; Xiao-Song Xie; Xiaochun Li

doi:10.1038/s41467-020-17762-9

Nature Communications (Aug 2020)

Cryo-EM structures of intact V-ATPase from bovine brain

Rong Wang,
Tao Long,
Abdirahman Hassan,
Jin Wang,
Yingyuan Sun,
Xiao-Song Xie,
Xiaochun Li

Affiliations

Rong Wang: Department of Molecular Genetics, University of Texas Southwestern Medical Center
Tao Long: Department of Molecular Genetics, University of Texas Southwestern Medical Center
Abdirahman Hassan: Department of Molecular Genetics, University of Texas Southwestern Medical Center
Jin Wang: Eugene McDermott Center for Human Growth and Development, University of Texas Southwestern Medical Center
Yingyuan Sun: Department of Molecular Genetics, University of Texas Southwestern Medical Center
Xiao-Song Xie: Eugene McDermott Center for Human Growth and Development, University of Texas Southwestern Medical Center
Xiaochun Li: Department of Molecular Genetics, University of Texas Southwestern Medical Center

DOI: https://doi.org/10.1038/s41467-020-17762-9
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 9

Abstract

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The vacuolar-type H+ -ATPases (V-ATPase) hydrolyze ATP to pump protons across the plasma or intracellular membrane. Here authors report two cryo-EM structures of the intact V-ATPase from bovine brain with all the subunits including the subunit H, which is essential for ATPase activity.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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