![]() Reconstitution of bacterial autotransporter assembly using purified components. Activation of cryptic aminoglycoside resistance in Salmonella enterica. Koskiniemi, S., Pranting, M., Gullberg, E., Nasvall, J. An efficient recombination system for chromosome engineering in Escherichia coli. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Regulation and mode of action of the second small RNA activator of RpoS translation, RprA. A small-molecule inhibitor of BamA impervious to efflux and the outer membrane permeability barrier. Chimeric peptidomimetic antibiotics against Gram-negative bacteria. A new antibiotic selectively kills Gram-negative pathogens. Monoclonal antibody targeting the beta-barrel assembly machine of Escherichia coli is bactericidal. Lateral opening and exit pore formation are required for BamA function. BamA beta16C strand and periplasmic turns are critical for outer membrane protein insertion and assembly. A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance. Mass spectrometry-enabled structural biology of membrane proteins. A disulfide bridge network within the soluble periplasmic domain determines structure and function of the outer membrane protein RCSF. Crystal structure of the outer membrane protein RcsF, a new substrate for the periplasmic protein-disulfide isomerase DsbC. Sequence-specific solution NMR assignments of the beta-barrel insertase BamA to monitor its conformational ensemble at the atomic level. Structural and functional analysis of the beta-barrel domain of BamA from Escherichia coli. Structure of BamA, an essential factor in outer membrane protein biogenesis. Identification of conformation-selective nanobodies against the membrane protein insertase BamA by an integrated structural biology approach. Distinct domains of Escherichia coli IgaA connect envelope stress sensing and down-regulation of the Rcs phosphorelay across subcellular compartments. Major Tom to ground control: how lipoproteins communicate extra-cytoplasmic stress to the decision center of the cell. The synthetic phenotype of deltabamb deltabame double mutants results from a lethal jamming of the bam complex by the lipoprotein RcsF. Improper coordination of BamA and BamD results in bam complex jamming by a lipoprotein substrate. Transmembrane domain of surface-exposed outer membrane lipoprotein RcsF is threaded through the lumen of beta-barrel proteins. Detecting envelope stress by monitoring beta-barrel assembly. ![]() Outer membrane protein folding from an energy landscape perspective. Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli. Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins. Structural basis of outer membrane protein insertion by the BAM complex. The structure of the beta-barrel assembly machinery complex. Lateral opening in the intact beta-barrel assembly machinery captured by cryo-EM. ![]() beta-Barrel membrane protein assembly by the Bam complex. The beta-barrel assembly machinery in motion. ![]()
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