7R1C

Cryo-EM structure of Bacillus megaterium gas vesicles

7R1C の概要

• エントリーDOI: 10.2210/pdb7r1c/pdb
• EMDBエントリー: 14238 14340
• 分子名称: Gas vesicle structural protein (1 entity in total)
• 機能のキーワード: gas vesicle, buoyancy, helical, microbial motility, structural protein
• 由来する生物種: Priestia megaterium NBRC 15308 = ATCC 14581
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9626.85

構造登録者

Huber, S.T.,Evers, W.,Jakobi, A.J. (登録日: 2022-02-02, 公開日: 2022-06-15, 最終更新日: 2024-07-17)

主引用文献

Huber, S.T.,Terwiel, D.,Evers, W.H.,Maresca, D.,Jakobi, A.J.
Cryo-EM structure of gas vesicles for buoyancy-controlled motility.
Cell, 186:975-986.e13, 2023

PubMed Abstract: Gas vesicles are gas-filled nanocompartments that allow a diverse group of bacteria and archaea to control their buoyancy. The molecular basis of their properties and assembly remains unclear. Here, we report the 3.2 Å cryo-EM structure of the gas vesicle shell made from the structural protein GvpA that self-assembles into hollow helical cylinders closed off by cone-shaped tips. Two helical half shells connect through a characteristic arrangement of GvpA monomers, suggesting a mechanism of gas vesicle biogenesis. The fold of GvpA features a corrugated wall structure typical for force-bearing thin-walled cylinders. Small pores enable gas molecules to diffuse across the shell, while the exceptionally hydrophobic interior surface effectively repels water. Comparative structural analysis confirms the evolutionary conservation of gas vesicle assemblies and demonstrates molecular features of shell reinforcement by GvpC. Our findings will further research into gas vesicle biology and facilitate molecular engineering of gas vesicles for ultrasound imaging.

PubMed: 36868215
DOI: 10.1016/j.cell.2023.01.041

実験手法

ELECTRON MICROSCOPY (3.2 Å)