The first crystal structure of an active plant asparaginyl endopeptidase reveals a tetrahedral intermediate state in its active site, which may help to explain why these enzymes have been independently recruited to perform peptide macrocyclization.

Peptidoglycan precursor synthesis occurs in both growing and non-growing regions of the mycobacterial cell surface.

The synthesis of bacterial cell wall peptidoglycan was reconstituted in lipid bilayers and detected by a novel Förster resonance energy transfer real-time assay.

Production of the L,D-transpeptidase YcbB and elevated synthesis of the (p)ppGpp alarmone reveals a new mode of peptidoglycan polymerization that bypasses the D,D-transpeptidase activity of PBPs and leads to broad-spectrum β-lactam resistance in Escherichia coli.

A single mutation in Escherichia coli connects two essential cell envelope assembly pathways and confers vancomycin resistance by displaying molecular decoys at the cell surface.

The helical bacterium Helicobacter pylori patterns cell wall synthesis using two distinct cytoskeletal proteins, CcmA and MreB, to achieve its characteristic shape.

The Braun lipoprotein is tethered to peptidoglycan independently from the insertion of newly-synthesized peptidoglycan subunits into the expanding cell wall generating a dynamic equilibrium between free and bound protein forms.

Allosteric mechanism of dual β-lactam binding in L,D-transpeptidase from Mycobacterium tuberculosis.

‘Optical tweezers’ measurements of single ribosomes and single mRNA molecules show that the translation rate depends exponentially on the applied force, and suggests that the ribosome functions as a Brownian ratchet.