A photo-sensitive amino acid analogue was introduced into an outer membrane lipoprotein, Pal, and then subjected to photo-crosslinking with the lipoprotein-specific ABC transporter LolCDE. Pal crosslinked to LolE but not LolC in vivo despite that both are structurally similar membrane subunits. LolCDE liganded with Pal containing the photo-sensitive amino acid analogue was isolated and subjected to in vitro photo-crosslinking. LolE was found to be the binding site for Pal. ATP binding to LolD decreased the LolE-Pal crosslinking by decreasing their hydrophobic interaction. ATP hydrolysis in the presence of LolA completely abolished the LolE-Pal crosslinking and, concomitantly, generated a new LolA-Pal crosslinked product.
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