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TitleCryo-EM structure of gas vesicles for buoyancy-controlled motility.
Journal, issue, pagesCell, Vol. 186, Issue 5, Page 975-986.e13, Year 2023
Publish dateMar 2, 2023
AuthorsStefan T Huber / Dion Terwiel / Wiel H Evers / David Maresca / Arjen J Jakobi /
PubMed AbstractGas 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, ...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.
External linksCell / PubMed:36868215 / PubMed Central
MethodsEM (helical sym.)
Resolution3.2 - 3.6 Å
Structure data

EMDB-14238, PDB-7r1c:
Cryo-EM structure of Bacillus megaterium gas vesicles
Method: EM (helical sym.) / Resolution: 3.2 Å

EMDB-14340: Cryo-EM structure of Bacillus megaterium gas vesicles
Method: EM (helical sym.) / Resolution: 3.6 Å

Source
  • priestia megaterium nbrc 15308 = atcc 14581 (bacteria)
KeywordsSTRUCTURAL PROTEIN / gas vesicle / buoyancy / helical / microbial motility

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