Asset Details
MbrlCatalogueTitleDetail
Do you wish to reserve the book?
Molecular mechanism of phospholipid transport at the bacterial outer membrane interface
by
Luo, Min
, Yeow, Jiang
, Chng, Shu-Sin
in
101/28
/ 38/70
/ 631/45/287/1194
/ 631/45/612/1237
/ 631/535/1258/1259
/ 82/16
/ 82/80
/ 82/83
/ Antibiotics
/ Asymmetry
/ Bacteria
/ Bacterial Outer Membrane - metabolism
/ Bacterial Outer Membrane Proteins - metabolism
/ Biological Transport
/ Cell Membrane - metabolism
/ E coli
/ Electrostatic properties
/ Escherichia coli - genetics
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - metabolism
/ Gram-negative bacteria
/ Humanities and Social Sciences
/ Lipid bilayers
/ Lipid Bilayers - metabolism
/ Lipids
/ Lipopolysaccharides
/ Lipopolysaccharides - metabolism
/ Membrane Lipids - metabolism
/ Membranes
/ Molecular modelling
/ multidisciplinary
/ Phospholipids
/ Phospholipids - metabolism
/ Recruitment
/ Science
/ Science (multidisciplinary)
/ Thinning
2023
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
You are currently in the queue to collect this book. You will be notified once it is your turn to collect the book.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Molecular mechanism of phospholipid transport at the bacterial outer membrane interface
by
Luo, Min
, Yeow, Jiang
, Chng, Shu-Sin
in
101/28
/ 38/70
/ 631/45/287/1194
/ 631/45/612/1237
/ 631/535/1258/1259
/ 82/16
/ 82/80
/ 82/83
/ Antibiotics
/ Asymmetry
/ Bacteria
/ Bacterial Outer Membrane - metabolism
/ Bacterial Outer Membrane Proteins - metabolism
/ Biological Transport
/ Cell Membrane - metabolism
/ E coli
/ Electrostatic properties
/ Escherichia coli - genetics
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - metabolism
/ Gram-negative bacteria
/ Humanities and Social Sciences
/ Lipid bilayers
/ Lipid Bilayers - metabolism
/ Lipids
/ Lipopolysaccharides
/ Lipopolysaccharides - metabolism
/ Membrane Lipids - metabolism
/ Membranes
/ Molecular modelling
/ multidisciplinary
/ Phospholipids
/ Phospholipids - metabolism
/ Recruitment
/ Science
/ Science (multidisciplinary)
/ Thinning
2023
Oops! Something went wrong.
While trying to remove the title from your shelf something went wrong :( Kindly try again later!
Do you wish to request the book?
Molecular mechanism of phospholipid transport at the bacterial outer membrane interface
by
Luo, Min
, Yeow, Jiang
, Chng, Shu-Sin
in
101/28
/ 38/70
/ 631/45/287/1194
/ 631/45/612/1237
/ 631/535/1258/1259
/ 82/16
/ 82/80
/ 82/83
/ Antibiotics
/ Asymmetry
/ Bacteria
/ Bacterial Outer Membrane - metabolism
/ Bacterial Outer Membrane Proteins - metabolism
/ Biological Transport
/ Cell Membrane - metabolism
/ E coli
/ Electrostatic properties
/ Escherichia coli - genetics
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - metabolism
/ Gram-negative bacteria
/ Humanities and Social Sciences
/ Lipid bilayers
/ Lipid Bilayers - metabolism
/ Lipids
/ Lipopolysaccharides
/ Lipopolysaccharides - metabolism
/ Membrane Lipids - metabolism
/ Membranes
/ Molecular modelling
/ multidisciplinary
/ Phospholipids
/ Phospholipids - metabolism
/ Recruitment
/ Science
/ Science (multidisciplinary)
/ Thinning
2023
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Molecular mechanism of phospholipid transport at the bacterial outer membrane interface
Journal Article
Molecular mechanism of phospholipid transport at the bacterial outer membrane interface
2023
Request Book From Autostore
and Choose the Collection Method
Overview
The outer membrane (OM) of Gram-negative bacteria is an asymmetric lipid bilayer with outer leaflet lipopolysaccharides and inner leaflet phospholipids (PLs). This unique lipid asymmetry renders the OM impermeable to external insults, including antibiotics and bile salts. To maintain this barrier, the OmpC-Mla system removes mislocalized PLs from the OM outer leaflet, and transports them to the inner membrane (IM); in the first step, the OmpC-MlaA complex transfers PLs to the periplasmic chaperone MlaC, but mechanistic details are lacking. Here, we biochemically and structurally characterize the MlaA-MlaC transient complex. We map the interaction surfaces between MlaA and MlaC in
Escherichia coli
, and show that electrostatic interactions are important for MlaC recruitment to the OM. We further demonstrate that interactions with MlaC modulate conformational states in MlaA. Finally, we solve a 2.9-Å cryo-EM structure of a disulfide-trapped OmpC-MlaA-MlaC complex in nanodiscs, reinforcing the mechanism of MlaC recruitment, and highlighting membrane thinning as a plausible strategy for directing lipids for transport. Our work offers critical insights into retrograde PL transport by the OmpC-Mla system in maintaining OM lipid asymmetry.
Maintenance of lipid asymmetry in the bacterial outer membrane (OM) is mediated by the OmpC-Mla system, but mechanistic details remain to be elucidated. Here, the authors show that electrostatic interactions, conformational dynamics, and membrane thinning may facilitate spontaneous retrograde phospholipid transfer at the OM.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 38/70
/ 82/16
/ 82/80
/ 82/83
/ Bacteria
/ Bacterial Outer Membrane - metabolism
/ Bacterial Outer Membrane Proteins - metabolism
/ E coli
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - metabolism
/ Humanities and Social Sciences
/ Lipids
/ Lipopolysaccharides - metabolism
/ Membrane Lipids - metabolism
/ Science
/ Thinning
This website uses cookies to ensure you get the best experience on our website.