PAS domains in bacterial signal transduction

PAS domains are widespread, versatile domains found in proteins from all kingdoms of life. The PAS fold is composed of an antiparallel beta-sheet with several flanking alpha-helices, and contains a conserved cleft for cofactor or ligand binding. The last few years have seen a prodigious increase in identified PAS domains and resolved PAS structures, including structures with effector and other domains. New bacterial PAS ligands have been discovered, and structure-function studies have improved our understanding of PAS signaling mechanisms. The list of bacterial PAS functions has now expanded to include roles in signal sensing, modulation, transduction, dimerization, protein interaction, and cellular localization.

Automated summary

PAS domains are versatile domains found in proteins across different kingdoms, with a conserved cleft for cofactor or ligand binding. Recent years have seen a significant increase in identified PAS domains and corresponding structures, leading to a better understanding of PAS signaling mechanisms. New bacterial PAS ligands have been discovered, expanding the list of bacterial PAS functions beyond signal sensing to include modulation, transduction, dimerization, protein interaction, and cellular localization.