Amilcar J. Perez

This study defines the substrate binding and activation mechanism of FtsW using simulations, mutagenesis, and assays, revealing conserved residues and structural constraints involved in lipid II binding and catalysis.

This paper identifies SddA, a periplasmic deacetylase that modulates daughter cell separation in E. coli by modifying denuded peptidoglycan strands, and links its function to amidase activation.

This study shows that the CRY2/CIB1 system can be used to precisely control protein localization in E. coli, enabling manipulation of cellular functions like cytokinesis.