7R1C

Cryo-EM structure of Bacillus megaterium gas vesicles

Summary for 7R1C

• Entry DOI: 10.2210/pdb7r1c/pdb
• EMDB information: 14238 14340
• Descriptor: Gas vesicle structural protein (1 entity in total)
• Functional Keywords: gas vesicle, buoyancy, helical, microbial motility, structural protein
• Biological source: Priestia megaterium NBRC 15308 = ATCC 14581
• Total number of polymer chains: 1
• Total formula weight: 9626.85

Authors

Huber, S.T.,Evers, W.,Jakobi, A.J. (deposition date: 2022-02-02, release date: 2022-06-15, Last modification date: 2024-07-17)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.2 Å)