Phospholipid translocation captured in a bifunctional membrane protein MprF

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...

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Main Authors: Danfeng Song, Haizhan Jiao, Zhenfeng Liu
Format: Article
Language:English
Published: Nature Publishing Group 2021-05-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-23248-z
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spelling doaj-2c1794c5fd6448e9afb654626ed56d7e2021-05-23T11:14:02ZengNature Publishing GroupNature Communications2041-17232021-05-0112111610.1038/s41467-021-23248-zPhospholipid translocation captured in a bifunctional membrane protein MprFDanfeng Song0Haizhan Jiao1Zhenfeng Liu2National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesThe 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).https://doi.org/10.1038/s41467-021-23248-z
collection DOAJ
language English
format Article
sources DOAJ
author Danfeng Song
Haizhan Jiao
Zhenfeng Liu
spellingShingle Danfeng Song
Haizhan Jiao
Zhenfeng Liu
Phospholipid translocation captured in a bifunctional membrane protein MprF
Nature Communications
author_facet Danfeng Song
Haizhan Jiao
Zhenfeng Liu
author_sort Danfeng Song
title Phospholipid translocation captured in a bifunctional membrane protein MprF
title_short Phospholipid translocation captured in a bifunctional membrane protein MprF
title_full Phospholipid translocation captured in a bifunctional membrane protein MprF
title_fullStr Phospholipid translocation captured in a bifunctional membrane protein MprF
title_full_unstemmed Phospholipid translocation captured in a bifunctional membrane protein MprF
title_sort phospholipid translocation captured in a bifunctional membrane protein mprf
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-05-01
description 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).
url https://doi.org/10.1038/s41467-021-23248-z
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AT haizhanjiao phospholipidtranslocationcapturedinabifunctionalmembraneproteinmprf
AT zhenfengliu phospholipidtranslocationcapturedinabifunctionalmembraneproteinmprf
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