Proteomics

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Structure of Anabaena flos-aquae gas vesicles revealed by cryo-ET


ABSTRACT: Gas Vesicles (GVs) are gas-filled protein nanostructures employed by several species of bacteria and archaea as flotation devices to enable access to optimal light and nutrients. The unique physical properties of GVs have led to their use as genetically-encodable contrast agents for ultrasound and MRI. Currently, however, the structure and assembly mechanism of GVs remain unknown. Here we employ cryo-electron tomography to reveal how the GV shell is formed by a helical filament of highly-conserved GvpA subunits. This filament changes polarity at the center of the GV cylinder, a site that may act as an elongation center. High-resolution subtomogram averaging reveals a corrugated pattern of the shell arising from polymerization of GvpA into a β-sheet. The accessory protein GvpC forms a helical cage around the GvpA shell, providing reinforcement. Together, our results help explain the remarkable mechanical properties of GVs and their ability to adopt different diameters and shapes.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Dolichospermum Flos-aquae 04-10

TISSUE(S): Cell Culture

SUBMITTER: Ting-Yu Wang  

LAB HEAD: Grant J. Jensen

PROVIDER: PXD038631 | Pride | 2023-03-30

REPOSITORIES: Pride

Dataset's files

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Prze_20220423_QE_BS3_crosslinks.xlsx Xlsx
Prze_20220423_QE_DSSO-crosslink.xlsx Xlsx
Przemyslaw_20220417_QE_Aur30min_BS3.raw Raw
Przemyslaw_20220417_QE_Aur30min_DSSO.raw Raw
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