Results 1 to 10 of about 202,274 (318)

Evolutionary pathways of repeat protein topology in bacterial outer membrane proteins. [PDF]

open access: yesElife, 2018
Outer membrane proteins (OMPs) are the proteins in the surface of Gram-negative bacteria. These proteins have diverse functions but a single topology: the β-barrel.
Franklin MW   +5 more
europepmc   +6 more sources

The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition. [PDF]

open access: greenJ Biol Chem, 2018
Most proteins that reside in the bacterial outer membrane (OM) have a distinctive “β-barrel” architecture, but the assembly of these proteins is poorly understood.
Hussain S, Bernstein HD.
europepmc   +3 more sources

Bacterial outer membrane proteins assemble via asymmetric interactions with the BamA β-barrel. [PDF]

open access: yesNat Commun, 2019
The integration of β-barrel proteins into the bacterial outer membrane (OM) is catalysed by the β-barrel assembly machinery (BAM). Here authors develop a method to trap an E.
Doyle MT, Bernstein HD.
europepmc   +3 more sources

Structure and function of bacterial outer membrane proteins: barrels in a nutshell [PDF]

open access: bronzeMolecular Microbiology, 2000
The outer membrane protects Gram‐negative bacteria against a harsh environment. At the same time, the embedded proteins fulfil a number of tasks that are crucial to the bacterial cell, such as solute and protein translocation, as well as signal transduction.
Ralf Koebnik   +2 more
semanticscholar   +5 more sources

Bacterial Outer Membrane Proteins Are Targeted to the Bam Complex by Two Parallel Mechanisms. [PDF]

open access: yesmBio, 2021
Proteins that are embedded in the outer membrane of Gram-negative bacteria (OMPs) play an important role in protecting the cell from harmful chemicals. OMPs share a architecture and often contain a conserved sequence motif (β motif) of unknown function ...
Wang X, Peterson JH, Bernstein HD.
europepmc   +2 more sources

How nanoscale protein interactions determine the mesoscale dynamic organisation of bacterial outer membrane proteins. [PDF]

open access: yesNat Commun, 2018
The spatiotemporal organisation of membranes is often characterised by the formation of large protein clusters. In Escherichia coli, outer membrane protein (OMP) clustering leads to OMP islands, the formation of which underpins OMP turnover and drives ...
Chavent M   +10 more
europepmc   +2 more sources

Inflammasome Activation by Bacterial Outer Membrane Vesicles Requires Guanylate Binding Proteins

open access: yesmBio, 2017
The Gram-negative bacterial cell wall component lipopolysaccharide (LPS) is recognized by the noncanonical inflammasome protein caspase-11 in the cytosol of infected host cells and thereby prompts an inflammatory immune response linked to sepsis.
Ryan Finethy   +8 more
doaj   +2 more sources

Dual recognition of multiple signals in bacterial outer membrane proteins enhances assembly and maintains membrane integrity. [PDF]

open access: yesElife
Outer membrane proteins (OMPs) are essential components of the outer membrane of Gram-negative bacteria. In terms of protein targeting and assembly, the current dogma holds that a ‘β-signal’ imprinted in the final β-strand of the OMP engages the β-barrel
Germany EM   +15 more
europepmc   +2 more sources

Solution nuclear magnetic resonance spectroscopy of bacterial outer membrane proteins in natively excreted vesicles using engineered Escherichia coli. [PDF]

open access: yesMicrobiologyopen, 2022
Gaining structural information on membrane proteins in their native lipid environment is a long‐standing challenge in molecular biology. Instead, it is common to employ membrane mimetics, which has been shown to affect protein structure, dynamics, and ...
Mouhib M, Chi CN.
europepmc   +2 more sources

Preparation of Bacterial Outer Membrane Vesicles for Characterisation of Periplasmic Proteins in Their Native Environment

open access: greenBio-Protocol, 2020
Bacterial outer membrane vesicles (OMVs) are naturally formed by budding from the outer membrane of Gram-negative bacteria. OMVs consist of a lipid bilayer identical in composition to the original outer membrane and contain periplasmic content within ...
Johannes Thoma, Björn Burmann
doaj   +3 more sources

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