Dual function of LapB (YciM) in regulating Escherichia coli lipopolysaccharide synthesis.

ABSTRACT: Levels of lipopolysaccharide (LPS), an essential glycolipid on the surface of most gram-negative bacteria, are tightly controlled-making LPS synthesis a promising target for developing new antibiotics. Escherichia coli adaptor protein LapB (YciM) plays an important role in regulating LPS synthesis by promoting degradation of LpxC, a deacetylase that catalyzes the first committed step in LPS synthesis. Under conditions where LPS is abundant, LapB recruits LpxC to the AAA+ protease FtsH for degradation. LapB achieves this by simultaneously interacting with FtsH through its transmembrane helix and LpxC through its cytoplasmic domain. Here, we describe a cryo-EM structure of the complex formed between LpxC and the cytoplasmic domain of LapB (LapB_cyto). The structure reveals h

SUBMITTER: Shu S 

PROVIDER: S-EPMC11046580 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature