Conformational switching in the coiled-coil domains of a proteasomal ATPase regulates substrate processing
Open accessAbstract
Protein degradation in all domains of life requires ATPases that unfold and inject proteins into compartmentalized proteolytic chambers. Proteasomal ATPases in eukaryotes and archaea contain poorly understood N-terminally conserved coiled-coil domains. In this study, we engineer disulfide crosslinks in the coiled-coils of the archaeal proteasomal ATPase (PAN) and report that its three identical coiled-coil domains can adopt three different conformations: (1) in-register and zipped, (2) in-register and partially unzipped, and (3) out-of-register. This conformational heterogeneity conflicts with PAN’s symmetrical OB-coiled-coil crystal structure but resembles the conformational heterogeneity of the 26S proteasomal ATPases’ coiled-coils. Furthermore, we find that one coiled-coil can be conformationally constrained even while unfolding substrates, and conformational changes in two of the coiled-coils regulate PAN switching between resting and active states. This switching functionally mimics similar states proposed for the 26S proteasome from cryo-EM. These findings thus build a mechanistic framework to understand regulation of proteasome activity.
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Natural coiled coils are dynamic and play central roles in a multitude of biological functions.
“Natural coiled coils, on the other hand, are dynamic and play central roles in a multitude of biological functions.13−17”
From Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints (2025) · cites this paper as [16]
The Introduction (page unavailable) says that some coiled coils undergo dynamic rearrangements that regulate protein function, and gives dynein as an example. It also notes that coiled coils occur in rigid structures, so it does not support the unqualified claim that natural coiled coils generally are dynamic or play central roles in a multitude of functions. (LLM, conf=0.86)
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Cui, H., Trybus, K., Ali, M. Y., Goyal, P., Aura, X. D., Loh, J., Noell, C. R., & Solmaz, S. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2019.11.2407
Noell, C. R., Loh, J., Debler, E., Loftus, K. M., Cui, H., Russ, B. B., Goyal, P., & Solmaz, S. (2019) · bioRxiv · doi:10.1101/638536
“22 Coiled-coil registry shifts have also been reported for other cases (Carter et al., 2008; Choi et al., 2011; Croasdale et al., 2011; Gibbons et al., 2005; Macheboeuf et al., 2011; Snoberger et al., 2018; Xi et al., 2012).”
BackgroundStepping up protein degradation
Maupin-Furlow, J. (2018) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1819949116
- Authors
- Snoberger, A., Brettrager, E. J., & Smith, D. M.
- Affiliations
- West Virginia University (US)
- Corresponding author
- Smith, David M.
- Venue
- Nature Communications
- Published
- 2018-06-18
- Volume
- 9
- Issue
- 1
- Pages
- 2374-2374
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC6006169
- OpenAlex
- W2807864108
- Cited by
- 30
- References
- 60
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 3 · 2023: 3 · 2022: 3 · 2021: 4 · 2020: 6 · 2019: 5 · 2018: 2
- FWCI
- 1.51
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- The Research Repository @ WVU (West Virginia University) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (R01GM107129)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- Pan, coiled-coil domain, conformational switching, disulfide cross-links, archaeal proteasome, substrate unfolding, proteasome activation, OB domain, 26S proteasome, protein degradation
- MeSH terms
- Protein Domains, Adenosine Triphosphatases, Thermoplasma, Proteasome Endopeptidase Complex
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