+Search query
-Structure paper
Title | Cryo-EM structures of LptBFG and LptBFGC from Klebsiella pneumoniae in complex with lipopolysaccharide. |
---|---|
Journal, issue, pages | Biochem Biophys Res Commun, Vol. 571, Page 20-25, Year 2021 |
Publish date | Sep 24, 2021 |
![]() | Qingshan Luo / Huigang Shi / Xueqing Xu / ![]() |
PubMed Abstract | Lipopolysaccharide (LPS) is an essential component of the outer membrane (OM) in most Gram-negative bacteria. LPS transport from the inner membrane (IM) to the OM is achieved by seven ...Lipopolysaccharide (LPS) is an essential component of the outer membrane (OM) in most Gram-negative bacteria. LPS transport from the inner membrane (IM) to the OM is achieved by seven lipopolysaccharide transport proteins (LptA-G). LptBFG, an type VI ATP-binding cassette (ABC) transporter, forms a stable complex with LptC, extracts LPS from the IM and powers LPS transport to the OM. Here we report the cryo-EM structures of LptBFG and LptBFGC from Klebsiella pneumoniae in complex with LPS. The KpLptBFG-LPS structure provides detailed interactions between LPS and the transporter, while the KpLptBFGC-LPS structure may represent an intermediate state that the transmembrane helix of LptC has not been fully inserted into the transmembrane domains of LptBFG. |
![]() | ![]() ![]() |
Methods | EM (single particle) |
Resolution | 3.85 Å |
Structure data | ![]() EMDB-31087: EMDB-31088, PDB-7efo: |
Chemicals | ![]() ChemComp-JSG: |
Source |
|
![]() | MEMBRANE PROTEIN / ABC transporter |