Rachel A. North

This study identifies how SpNanR activates sialic acid metabolism in S. pneumoniae by binding N-acetylmannosamine-6-phosphate, stabilizing its tetramer and enhancing transcription of the nan and siaA operons.

This study identifies TAM as a bacterial phospholipid transport system, revealing its structure and mechanism for lipid delivery to the outer membrane.

This study solves the structure of the TRAP substrate-binding protein AaSiaP in different conformations, revealing how it binds N-acetylneuraminate and stabilizes a closed state.

This study reports the cryo-EM structure of a TRAP transporter from Haemophilus influenzae, revealing its dimeric architecture, Na+ sites, and substrate binding site, supported by mutagenic and functional data.

The paper reports the cryo-EM structure of a TRAP transporter and elucidates its mechanism of sodium-driven substrate uptake.

This study elucidates how NanR represses sialic acid metabolism in E. coli by showing its cooperative DNA binding and allosteric regulation by N-acetylneuraminate.