Kathleen Postle

The paper validates aspects of the TonB system working model through in vivo experiments, identifying new ExbB-interacting proteins and PMF-dependent ExbD conformational changes.

This paper investigates the Escherichia coli ExbD transmembrane domain, identifies key residues for TonB system activity, and demonstrates that a cyclic peptide can inhibit ExbD-TonB interaction, suggesting a potential antimicrobial strategy.

This study identifies new in vivo interaction sites between TonB and the TBDT FepA using disulfide crosslinking, revealing distinct roles for different TonB regions in cork movement and TBDT recognition.