7OMM

Cryo-EM structure of N. gonorhoeae LptDE in complex with ProMacrobodies (MBPs have not been built de novo)

7OMM の概要

• エントリーDOI: 10.2210/pdb7omm/pdb
• EMDBエントリー: 12990
• 分子名称: LPS-assembly protein LptD, LPS-assembly lipoprotein LptE, ProMacrobody 21,Maltodextrin-binding protein, ... (4 entities in total)
• 機能のキーワード: outer membrane protein lps transporter bacterial transporter neisseria gonorrhoeae drug target promacrobodies structural chaperone cryo-electron microscopy, transport protein
• 由来する生物種: Neisseria gonorrhoeae; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 219732.04

構造登録者

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. (登録日: 2021-05-24, 公開日: 2022-05-04, 最終更新日: 2024-10-23)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (3.4 Å)