Bacterial cell surface glycoconjugates are critical for cell survival and for interactions between bacteria and their hosts.Consequently, the pathways responsible for their biosynthesis have untapped potential as therapeutic targets.The localization of many glycoconjugate biosynthesis enzymes to the membrane represents a significant challenge saint michael one piece shirt for expressing, purifying, and characterizing these enzymes.Here, we leverage cutting-edge detergent-free methods to stabilize, purify, and structurally characterize WbaP, a phosphoglycosyl transferase (PGT) from the Salmonella enterica (LT2) O-antigen biosynthesis.From a functional perspective, these studies establish WbaP as a homodimer, reveal the structural elements responsible for dimerization, shed light on the regulatory role of a domain of unknown function embedded within WbaP, and identify conserved structural motifs between PGTs and functionally unrelated UDP-sugar dehydratases.
From a technological perspective, the strategy developed here is generalizable and provides a toolkit for studying other blue kansas city chiefs hat classes of small membrane proteins embedded in liponanoparticles beyond PGTs.