Evolutionary pathways of repeat protein topology in bacterial outer membrane proteins [PDF]
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.
Meghan Whitney Franklin +5 more
doaj +4 more sources
Insertion of proteins and lipopolysaccharide into the bacterial outer membrane [PDF]
The bacterial outer membrane contains phospholipids in the inner leaflet and lipopolysaccharide (LPS) in the outer leaflet. Both proteins and LPS must be frequently inserted into the outer membrane to preserve its integrity. The protein complex that inserts LPS into the outer membrane is called LptDE, and consists of an integral membrane protein, LptD,
Nicholas Noinaj +2 more
exaly +3 more sources
Entry and exit of bacterial outer membrane proteins. [PDF]
The sites of new outer membrane protein (OMP) deposition and the fate of pre-existing OMPs are still enigmatic despite numerous concerted efforts. Rassam et al. identified mid-cell regions as the primary entry points for new OMP insertion in clusters, driving the pre-existing OMP clusters towards cell poles for long-term storage.
Misra R.
europepmc +3 more sources
Solution nuclear magnetic resonance spectroscopy of bacterial outer membrane proteins in natively excreted vesicles using engineered Escherichia coli [PDF]
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 ...
Mohammed Mouhib, Celestine N. Chi
doaj +2 more sources
Dual recognition of multiple signals in bacterial outer membrane proteins enhances assembly and maintains membrane integrity [PDF]
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
Edward M Germany +15 more
doaj +2 more sources
Extraction and Electrophoretic Analysis of Bacterial Lipopolysaccharides and Outer Membrane Proteins
Lipopolysaccharides (LPS) (or lipooligosaccharides [LOS], which lack the O-antigen side chains characteristic of LPS), and outer membrane proteins (OMP) are major cell-surface molecules in the outer membrane (OM) of gram-negative bacteria.
Yue Lee, Thomas Inzana
doaj +3 more sources
Not All Bacterial Outer-Membrane Proteins Are β-Barrels. [PDF]
The discovery of Wza, an octomeric helical barrel integral bacterial outer-transmembrane protein, has challenged the widely held understanding that all integral outer-membrane proteins of Gram-negative bacteria are closed β-barrels composed of transmembrane β- strands.
Heido J +4 more
europepmc +3 more sources
Bacterial outer membrane proteins assemble via asymmetric interactions with the BamA β-barrel [PDF]
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.
Matthew T. Doyle, Harris D. Bernstein
doaj +2 more sources
Protein-protein interactions and the spatiotemporal dynamics of bacterial outer membrane proteins.
It has until recently been unclear whether outer membrane proteins (OMPs) of Gram-negative bacteria are organized or distributed randomly. Studies now suggest promiscuous protein-protein interactions (PPIs) between β-barrel OMPs in Escherichia coli govern their local and global dynamics, engender spatiotemporal patterning of the outer membrane into ...
Kleanthous C, Rassam P, Baumann CG.
europepmc +3 more sources
Living on the edge: Simulations of bacterial outer-membrane proteins
Gram-negative bacteria are distinguished in part by a second, outer membrane surrounding them. This membrane is distinct from others, possessing an outer leaflet composed not of typical phospholipids but rather large, highly charged molecules known as lipopolysaccharides.
James C Gumbart +2 more
exaly +3 more sources

