Structural basis of the P4B ATPase lipid flippase activity

Lin Bai; Bhawik K. Jain; Qinglong You; H. Diessel Duan; Mehmet Takar; Todd R. Graham; Huilin Li

doi:10.1038/s41467-021-26273-0

Nature Communications (Oct 2021)

Structural basis of the P4B ATPase lipid flippase activity

Lin Bai,
Bhawik K. Jain,
Qinglong You,
H. Diessel Duan,
Mehmet Takar,
Todd R. Graham,
Huilin Li

Affiliations

Lin Bai: Department of Biochemistry and Biophysics, School of Basic Medical Sciences, Peking University
Bhawik K. Jain: Department of Biological Sciences, Vanderbilt University
Qinglong You: Department of Structural Biology, Van Andel Institute
H. Diessel Duan: Department of Structural Biology, Van Andel Institute
Mehmet Takar: Department of Biological Sciences, Vanderbilt University
Todd R. Graham: Department of Biological Sciences, Vanderbilt University
Huilin Li: Department of Structural Biology, Van Andel Institute

DOI: https://doi.org/10.1038/s41467-021-26273-0
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 12

Abstract

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The P4 ATPase lipid flippases play a crucial role in membrane biogenesis. Here the authors report the structure of the monomeric P4B ATPase Neo1 in several states, clarifying the mechanism of substrate transport.

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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