β-Barrel Assembly Machinery (BAM) Complex as Novel Antibacterial Drug Target [PDF]
The outer membrane of Gram-negative bacteria is closely related to the pathogenicity and drug resistance of bacteria. Outer membrane proteins (OMPs) are a class of proteins with important biological functions on the outer membrane.
Qian Xu, Min Guo, Feiyuan Yu
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Structure of a nascent membrane protein as it folds on the BAM complex. [PDF]
Mitochondria, chloroplasts and Gram-negative bacteria are encased in a double layer of membranes. The outer membrane contains proteins with a β-barrel structure1,2. β-Barrels are sheets of β-strands wrapped into a cylinder, in which the first strand is hydrogen-bonded to the final strand. Conserved multi-subunit molecular machines fold and insert these
Tomasek D +6 more
europepmc +7 more sources
Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs [PDF]
With cryo-EM, single-molecule FRET and MD simulations, Iadanza et al. characterise the membrane protein insertase complex BAM in lipid bilayer nanodiscs.
Matthew G. Iadanza +11 more
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Reconstitution of Bam Complex-Mediated Assembly of a Trimeric Porin into Proteoliposomes. [PDF]
Porins are a widespread family of homotrimers that represent a substantial fraction of the total protein located in the OM of many proteobacteria. These proteins facilitate the nonspecific diffusion of small molecules across the outer membrane and strongly influence the susceptibility of bacteria to clinically used antibiotics.
Hussain S, Peterson JH, Bernstein HD.
europepmc +4 more sources
Overproducing the BAM complex improves secretion of difficult-to-secrete recombinant autotransporter chimeras. [PDF]
AbstractMonomeric autotransporters have been used extensively to transport recombinant proteins or protein domains to the cell surface of Gram-negative bacteria amongst others for antigen display. Genetic fusion of such antigens into autotransporters has yielded chimeras that can be used for vaccination purposes.
Phan TH +5 more
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Darobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex in E. coli Cells. [PDF]
AbstractThe β‐barrel assembly machinery (BAM complex) is essential for outer membrane protein (OMP) folding in Gram‐negative bacteria, and represents a promising antimicrobial target. Several conformational states of BAM have been reported, but all have been obtained under conditions which lack the unique features and complexity of the outer membrane ...
Haysom SF +11 more
europepmc +7 more sources
Bacterial Outer Membrane Proteins Are Targeted to the Bam Complex by Two Parallel Mechanisms. [PDF]
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 +4 more sources
Combining Cell Envelope Stress Reporter Assays in a Screening Approach to Identify BAM Complex Inhibitors. [PDF]
The development of new antibiotics is particularly problematic in Gram-negative bacteria due to the presence of the outer membrane (OM), which serves as a permeability barrier. Recently, the β-barrel assembly machine (BAM), located in the OM and responsible for β-barrel type OM protein (OMP) assembly, has been validated as a novel target for ...
Steenhuis M +9 more
europepmc +7 more sources
Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM [PDF]
The β-barrel assembly machinery (BAM complex) is a key mediator of outer membrane protein biogenesis in Gram-negative bacteria. Here the authors report a cryo-EM structure of the intact BAM complex that suggests that lateral gate opening is a necessary ...
Matthew G. Iadanza +7 more
doaj +2 more sources
Classifying β-Barrel Assembly Substrates by Manipulating Essential Bam Complex Members. [PDF]
ABSTRACT The biogenesis of the outer membrane (OM) of Escherichia coli is a conserved and vital process. The assembly of integral β-barrel outer membrane proteins (OMPs), which represent a major component of the OM, depends on periplasmic chaperones and the heteropentameric β-barrel assembly machine (Bam ...
Mahoney TF, Ricci DP, Silhavy TJ.
europepmc +4 more sources

