7OMT

Crystal structure of ProMacrobody 21 with bound maltose

Summary for 7OMT

• Entry DOI: 10.2210/pdb7omt/pdb
• Related: 7OMM
• EMDB information: 12990
• Related PRD ID: PRD_900001
• Descriptor: ProMacrobody 21, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, HEXAETHYLENE GLYCOL, ... (5 entities in total)
• Functional Keywords: nanobody cryo-em chaperone mbp, immune system
• Biological source: synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 57645.72

Authors

Botte, M.,Ni, D.,Schenck, S.,Zimmermann, I.,Chami, M.,Bocquet, N.,Egloff, P.,Bucher, D.,Trabuco, M.,Cheng, R.K.Y.,Brunner, J.D.,Seeger, M.A.,Stahlberg, H.,Hennig, M. (deposition date: 2021-05-24, release date: 2022-05-04, Last modification date: 2024-11-20)

Primary citation

Botte, M.,Ni, D.,Schenck, S.,Zimmermann, I.,Chami, M.,Bocquet, N.,Egloff, P.,Bucher, D.,Trabuco, M.,Cheng, R.K.Y.,Brunner, J.D.,Seeger, M.A.,Stahlberg, H.,Hennig, M.
Cryo-EM structures of a LptDE transporter in complex with Pro-macrobodies offer insight into lipopolysaccharide translocation.
Nat Commun, 13:1826-1826, 2022

PubMed 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.

PubMed: 35383177
DOI: 10.1038/s41467-022-29459-2

Experimental method

X-RAY DIFFRACTION (2 Å)