Phospholipid translocation captured in a bifunctional membrane protein MprF

Danfeng Song; Haizhan Jiao; Zhenfeng Liu

doi:10.1038/s41467-021-23248-z

Nature Communications (May 2021)

Phospholipid translocation captured in a bifunctional membrane protein MprF

Danfeng Song,
Haizhan Jiao,
Zhenfeng Liu

Affiliations

Danfeng Song: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
Haizhan Jiao: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
Zhenfeng Liu: National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences

DOI: https://doi.org/10.1038/s41467-021-23248-z
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 16

Abstract

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The Multiple Peptide Resistance Factors (MprFs) utilize two separate domains to synthesize and translocate aminoacyl phospholipids to the outer leaflets of bacterial membranes. Here authors present cryo-electron microscopy structures of MprF homodimer from Rhizobium tropici (RtMprF) at two different states in complex with lysyl-phosphatidylglycerol (LysPG).

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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