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Cryo-EM structure of the diapause chaperone artemin
Open accessPreprint — published as 10.3389/fmolb.2022.998562 · Paper page
Abstract
The protein artemin constitutes over 10% of all protein in Artemia cysts during diapause and acts as both an RNA and protein chaperone. However, its mechanistic details remain elusive since no high-resolution structure of artemin exists. Here we report the full-length structure of artemin at 2.04 Å resolution. The cryo-EM map contains density for an intramolecular disulfide bond between Cys22-Cys61 and resolves the entire C-terminus extending into the core of the assembled protein cage. We also provide data supporting the role of C-terminal helix F towards stabilizing the dimer form that is believed to be important for its chaperoning activity. We were able to destabilize this effect by placing a tag at the C-terminus to fully pack the internal cavity and cause limited steric hindrance.
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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
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Metadata
- Authors
- Parvate, A. D., Powell, S. M., Brookreson, J. T., Moser, T. H., Novikova, I. V., Zhou, M., & Evans, J. E.
- Affiliations
- Pacific Northwest National Laboratory (US)
- Corresponding author
- Evans, James E.
- ORCID
- Venue
- Frontiers in Molecular Biosciences
- Publisher
- openRxiv
- Published
- 2022-04-06
- Volume
- 9
- Pages
- 998562-998562
- ISSN
- 2296-889X (ISSN-L)
- PMC
- PMC9742257
- OpenAlex
- W4310266620
- Cited by
- 5
- References
- 1
- Citations by year
- 2025: 3 · 2024: 2
- FWCI
- 0.41
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Frontiers in Molecular Biosciences (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- U.S. Department of Energy (FWP74915, grid.436923.9, 436923.9)
- Office of Science (grid.436923.9)
- Biological and Environmental Research (FWP 74915, 74915, grid.436923.9)
- Pacific Northwest National Laboratory
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- artemin, diapause, molecular chaperones, protein structure, intramolecular disulfide bond, C-terminal helix, protein dimerization, cysts, protein cages, steric hindrance
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