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TitleCryo-EM structures of a LptDE transporter in complex with Pro-macrobodies offer insight into lipopolysaccharide translocation.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 1826, Year 2022
Publish dateApr 5, 2022
AuthorsMathieu Botte / Dongchun Ni / Stephan Schenck / Iwan Zimmermann / Mohamed Chami / Nicolas Bocquet / Pascal Egloff / Denis Bucher / Matilde Trabuco / Robert K Y Cheng / Janine D Brunner / Markus A Seeger / Henning Stahlberg / Michael Hennig /
PubMed AbstractLipopolysaccharides are major constituents of the extracellular leaflet in the bacterial outer membrane and form an effective physical barrier for environmental threats and for antibiotics in Gram- ...Lipopolysaccharides are major constituents of the extracellular leaflet in the bacterial outer membrane and form an effective physical barrier for environmental threats and for antibiotics in Gram-negative bacteria. The last step of LPS insertion via the Lpt pathway is mediated by the LptD/E protein complex. Detailed insights into the architecture of LptDE transporter complexes have been derived from X-ray crystallography. However, no structure of a laterally open LptD transporter, a transient state that occurs during LPS release, is available to date. Here, we report a cryo-EM structure of a partially opened LptDE transporter in complex with rigid chaperones derived from nanobodies, at 3.4 Å resolution. In addition, a subset of particles allows to model a structure of a laterally fully opened LptDE complex. Our work offers insights into the mechanism of LPS insertion, provides a structural framework for the development of antibiotics targeting LptD and describes a highly rigid chaperone scaffold to enable structural biology of challenging protein targets.
External linksNat Commun / PubMed:35383177 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2 - 3.4 Å
Structure data

12990

7omm

EMDB-12990: Cryo-EM structure of N. gonorhoeae LptDE in complex with ProMacrobodies
PDB-7omm: Cryo-EM structure of N. gonorhoeae LptDE in complex with ProMacrobodies (MBPs have not been built de novo)
Method: EM (single particle) / Resolution: 3.4 Å

PDB-7omt:
Crystal structure of ProMacrobody 21 with bound maltose
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-P6G:
HEXAETHYLENE GLYCOL / precipitant*YM

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • neisseria gonorrhoeae (bacteria)
  • methanosarcina mazei (archaea)
  • synthetic construct (others)
KeywordsTRANSPORT PROTEIN / Outer membrane protein LPS transporter Bacterial transporter Neisseria gonorrhoeae Drug target ProMacrobodies Structural chaperone Cryo-electron microscopy / IMMUNE SYSTEM / nanobody Cryo-EM Chaperone MBP

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