David Tomasek

TL;DR: Crystal structures of ArnT from Cupriavidus metallidurans, alone and in complex with the lipid carrier undecaprenyl phosphate, are reported and functional mutagenesis experiments suggest a mechanistic model for ArnT family enzymes.

TL;DR: Cryo-electron microscopy structures of a folding intermediate on the BAM complex of Escherichia coli reveal how interactions between the BamA catalyst and substrate permit stable association during folding, followed by rapid turnover.

TL;DR: A cell-based screen that identifies inhibitors of LPS biosynthesis and transport by exploiting the nonessentiality of this pathway in Acinetobacter, and validates MsbA as an antibacterial target.

TL;DR: It is concluded that substrate binding to BamD activates BamA by regulating extracellular loop interactions for folding and membrane integration, and could enable the design of strategies to combat Gram-negative pathogens.

TL;DR: The path of substrate insertion by the Bam complex is mapped using site-specific crosslinking to understand the molecular mechanisms that control β-barrel folding and release and identifies contacts between the assembling β-sheet and the BamA interior surface that determine the rate of substrate folding.