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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2021-05-01
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Online Access: | https://doi.org/10.1038/s41467-021-23248-z |
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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 |
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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 |
work_keys_str_mv |
AT danfengsong phospholipidtranslocationcapturedinabifunctionalmembraneproteinmprf AT haizhanjiao phospholipidtranslocationcapturedinabifunctionalmembraneproteinmprf AT zhenfengliu phospholipidtranslocationcapturedinabifunctionalmembraneproteinmprf |
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1724163656605761536 |