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-Structure paper
Title | Regulatory mechanisms of lipopolysaccharide synthesis in Escherichia coli. |
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Journal, issue, pages | Nat Commun, Vol. 13, Issue 1, Page 4576, Year 2022 |
Publish date | Aug 5, 2022 |
![]() | Sheng Shu / Wei Mi / ![]() |
PubMed Abstract | Lipopolysaccharide (LPS) is an essential glycolipid and forms a protective permeability barrier for most Gram-negative bacteria. In E. coli, LPS levels are under feedback control, achieved by FtsH- ...Lipopolysaccharide (LPS) is an essential glycolipid and forms a protective permeability barrier for most Gram-negative bacteria. In E. coli, LPS levels are under feedback control, achieved by FtsH-mediated degradation of LpxC, which catalyzes the first committed step in LPS synthesis. FtsH is a membrane-bound AAA+ protease, and its protease activity toward LpxC is regulated by essential membrane proteins LapB and YejM. However, the regulatory mechanisms are elusive. We establish an in vitro assay to analyze the kinetics of LpxC degradation and demonstrate that LapB is an adaptor protein that utilizes its transmembrane helix to interact with FtsH and its cytoplasmic domains to recruit LpxC. Our YejM/LapB complex structure reveals that YejM is an anti-adaptor protein, competing with FtsH for LapB to inhibit LpxC degradation. Structural analysis unravels that LapB and LPS have overlapping binding sites in YejM. Thus, LPS levels control formation of the YejM/LapB complex to determine LpxC protein levels. |
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Methods | EM (single particle) |
Resolution | 3.9 - 4.1 Å |
Structure data | EMDB-25713, PDB-7t6d: ![]() EMDB-25731: CryoEM map of the YejM/LapB complex with periplasmic domain |
Chemicals | ![]() ChemComp-LPP: ![]() ChemComp-PGV: |
Source |
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![]() | MEMBRANE PROTEIN / YejM / YciM / regulation / lipopolysaccharide synthesis / LpxC |