Cryo-EM structures of a LptDE transporter in complex with Pro-macrobodies offer insight into lipopolysaccharide translocation

Mathieu 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 and Michael Hennig ()
Additional contact information
Mathieu Botte: leadXpro AG, Park Innovaare
Dongchun Ni: University of Basel
Stephan Schenck: leadXpro AG, Park Innovaare
Iwan Zimmermann: University of Zürich
Mohamed Chami: University of Basel
Nicolas Bocquet: leadXpro AG, Park Innovaare
Pascal Egloff: University of Zürich
Denis Bucher: leadXpro AG, Park Innovaare
Matilde Trabuco: leadXpro AG, Park Innovaare
Robert K. Y. Cheng: leadXpro AG, Park Innovaare
Janine D. Brunner: Paul Scherrer Institute (PSI)
Markus A. Seeger: University of Zürich
Henning Stahlberg: University of Basel
Michael Hennig: leadXpro AG, Park Innovaare

Nature Communications, 2022, vol. 13, issue 1, 1-10

Abstract: Abstract 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.

Date: 2022
References: View references in EconPapers View complete reference list from CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/s41467-022-29459-2 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-29459-2

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-022-29459-2

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().