Structure of Anabaena flos-aquae gas vesicles revealed by cryo-ET
Open accessPublished version of a preprint
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.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
ColabFold - Making protein folding accessible to all
Mirdita, M., Schütze, K., Moriwaki, Y., Heo, L., Ovchinnikov, S., & Steinegger, M. (2021) · doi:10.1101/2021.08.15.456425 · Cited by 9,391 · see citing works
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- Authors
- Dutka, 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.
- Affiliations
- California Institute of Technology (US)
- Brigham Young University (US)
- Corresponding author
- Shapiro, Mikhail G.
- Jensen, Grant J.
- ORCID
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2023-05
- Volume
- 31
- Issue
- 5
- Pages
- 518-528.e6
- ISSN
- 0969-2126 (ISSN-L)
- PMC
- PMC10185304
- OpenAlex
- W4363675958
- Cited by
- 51
- References
- 2
- Citations by year
- 2026: 10 · 2025: 15 · 2024: 17 · 2023: 8 · 2022: 1
- FWCI
- 4.42
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Structure (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion, cc-by)
- Zenodo (CERN European Organization for Nuclear Research) (submittedVersion, cc-by)
- Funders
- David and Lucile Packard Foundation
- Center for Environmental Microbial Interactions, California Institute of Technology
- National Institutes of Health (R01-EB018975, 1S10OD02001301, R01-AI127401)
- Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana-Champaign
- Heritage Medical Research Institute
- HHMI
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- gas vesicles, Anabaena flos-aquae, helical filaments, assembly mechanism, subtomogram averaging, cryo-electron tomography
- MeSH terms
- Archaea, Bacterial Proteins, Anabaena, Dolichospermum flos-aquae
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