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Structure of MlaFEDB ABC transporter with substrate bound in the outward-open pocket of MlaE provides mechanistic insights into lipid transport within the Gram-negative bacterial cell envelope.

Modulation of cytoplasmic lipopolysaccharide levels sensitises bacteria to polymyxin antibiotics, revealing a novel combination therapeutic approach.

Structural analysis of the type IV secretion system purified from Legionella pneumophila uncovers new complex components and symmetry mismatches.

Crystallography and single particle cryo-EM reveal hexameric and pentameric structures of the ExbBD energizer in the Ton system and oligomeric transition, which provides a unique working mechanism and a new vision of dynamic membrane biology.

Pulse electron paramagnetic resonance on intact Escherichia coli reveals a substrate-induced structural transition in BtuB, the vitamin B₁₂ transporter, which is not seen in reconstituted membranes and indicates a mechanism of transport.

The structure, function and mechanism of the malaria vaccine candidate CelTOS reveal a unique pore-forming and membrane-disrupting protein with specificity for the inner leaflet of host and vector cells.

Outer membrane β-barrel proteins in Gram-negative bacteria are assembled within the lumen of the BamA β-barrel.

Analysis of the E. coli protein DolP reveals the first dual BON-domain structure and identifies phospholipid binding as a new mechanism for protein localisation to the outer membrane division site.

Structures of CdiB outer membrane transporters reveal the channel-gating mechanism for the secretion of large bacterial toxins.

Both beneficial and pathogenic bacteria can use their sheathed flagella during host colonization as a novel toxin-/signal-delivery mechanism.