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8GBS

Integrative model of the native Ana GV shell

This is a non-PDB format compatible entry.
Summary for 8GBS
Entry DOI10.2210/pdb8gbs/pdb
EMDB information29921 29922 29923 29924 29925
DescriptorGas vesicle structural protein, Gas vesicle protein C (2 entities in total)
Functional Keywordsgas vesicles, flotation, cyanobacteria, cytosolic protein
Biological sourceDolichospermum flos-aquae (Anabaena flos-aquae)
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Total number of polymer chains5
Total formula weight32965.36
Authors
Dutka, P.,Metskas, L.A.,Hurt, R.C.,Salahshoor, H.,Wang, T.U.,Malounda, D.,Lu, G.,Chou, T.F.,Shapiro, M.G.,Jensen, J.J. (deposition date: 2023-02-28, release date: 2023-04-19, Last modification date: 2024-06-19)
Primary citationDutka, P.,Metskas, L.A.,Hurt, R.C.,Salahshoor, H.,Wang, T.Y.,Malounda, D.,Lu, G.J.,Chou, T.F.,Shapiro, M.G.,Jensen, G.J.
Structure of Anabaena flos-aquae gas vesicles revealed by cryo-ET.
Structure, 31:518-528.e6, 2023
Cited by
PubMed 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 cryoelectron 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. 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 structural reinforcement. Together, our results help explain the remarkable mechanical properties of GVs and their ability to adopt different diameters and shapes.
PubMed: 37040766
DOI: 10.1016/j.str.2023.03.011
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (8 Å)
Structure validation

238895

数据于2025-07-16公开中

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