8PBY

Single particle cryo-EM of the P140-P110 heterodimer with an alternative conformation in the P140 stalk of Mycoplasma genitalium at a resolution of 3.7 Angstrom.

8PBY の概要

• エントリーDOI: 10.2210/pdb8pby/pdb
• 関連するPDBエントリー: 6R3T 6RUT 8PBX
• EMDBエントリー: 17587 17588
• 分子名称: Mgp-operon protein 3, Adhesin P1 (2 entities in total)
• 機能のキーワード: adhesion, mycoplasma genitalium, cell adhesion
• 由来する生物種: Mycoplasmoides genitalium G37; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 275191.36

構造登録者

Sprankel, L.,Scheffer, M.P.,Frangakis, A.S. (登録日: 2023-06-09, 公開日: 2023-11-01, 最終更新日: 2023-11-22)

主引用文献

Sprankel, L.,Scheffer, M.P.,Manger, S.,Ermel, U.H.,Frangakis, A.S.
Cryo-electron tomography reveals the binding and release states of the major adhesion complex from Mycoplasma genitalium.
Plos Pathog., 19:e1011761-e1011761, 2023

PubMed Abstract: The nap particle is an immunogenic surface adhesion complex from Mycoplasma genitalium. It is essential for motility and responsible for binding sialylated oligosaccharides on the surface of the host cell. The nap particle is composed of two P140-P110 heterodimers, the structure of which was recently solved. However, the interpretation of the mechanism by which the mycoplasma cells orchestrate adhesion remained challenging. Here, we provide cryo-electron tomography structures at ~11 Å resolution, which allow for the distinction between the bound and released state of the nap particle, displaying the in vivo conformational states. Fitting of the atomically resolved structures reveals that bound sialylated oligosaccharides are stabilized by both P110 and P140. Movement of the stalk domains allows for the transfer of conformational changes from the interior of the cell to the binding pocket, thus having the capability of an active release process. It is likely that the same mechanism can be transferred to other Mycoplasma species that belong to the pneumoniae cluster.

PubMed: 37939157
DOI: 10.1371/journal.ppat.1011761

実験手法

ELECTRON MICROSCOPY (3.7 Å)