The lipopolysaccharide-transporter complex LptB₂FG also displays adenylate kinase activity in vitro dependent on the binding partners LptC/LptA.

ABSTRACT: Lipopolysaccharide (LPS) is an essential glycolipid that covers the surface of gram-negative bacteria. The transport of LPS involves a dedicated seven-protein transporter system called the lipopolysaccharide transport system (Lpt) machinery that physically spans the entire cell envelope. The LptB₂FG complex is an ABC transporter that hydrolyzes ATP to extract LPS from the inner membrane for transport to the outer membrane. Here, we extracted LptB₂FG directly from the inner membrane with its original lipid environment using styrene-maleic acid polymers. We found that styrene-maleic acid polymers-LptB₂FG in nanodiscs display not only ATPase activity but also a previously uncharacterized adenylate kinase (AK) activity, as it catalyzed phosphotransfer between t

SUBMITTER: Baeta T 

PROVIDER: S-EPMC8633020 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature