BIRC7–E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer
Open accessAbstract
Certain RING ubiquitin ligases (E3s) dimerize to facilitate ubiquitin (Ub) transfer from ubiquitin-conjugating enzyme (E2) to substrate, but structural evidence on how this process promotes Ub transfer is lacking. Here we report the structure of the human dimeric RING domain from BIRC7 in complex with the E2 UbcH5B covalently linked to Ub (UbcH5B∼Ub). The structure reveals extensive noncovalent donor Ub interactions with UbcH5B and both subunits of the RING domain dimer that stabilize the globular body and C-terminal tail of Ub. Mutations that disrupt these noncovalent interactions or RING dimerization reduce UbcH5B∼Ub binding affinity and ubiquitination activity. Moreover, NMR analyses demonstrate that BIRC7 binding to UbcH5B∼Ub induces peak-shift perturbations in the donor Ub consistent with the crystallographically-observed Ub interactions. Our results provide structural insights into how dimeric RING E3s recruit E2∼Ub and optimize the donor Ub configuration for transfer.
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Compared to prior isolated RING-UBE2D~UB structures, the neddylated CRL1β-TRCP-UBE2D~UB-substrate intermediate shows additional density corresponding to the substrate proxy along a trajectory to the ubiquitylation active site.
“Compared to prior isolated RING-UBE2D~UB structures28–30, the neddylated CRL1β-TRCP-UBE2D~UB-substrate intermediate shows additional density corresponding to the substrate proxy along a trajectory to the ubiquitylation active site”
From NEDD8 nucleates a multivalent cullin–RING–UBE2D ubiquitin ligation assembly (2020) · cites this paper as [28]
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- Authors
- Dou, H., Buetow, L., Sibbet, G. J., Cameron, K., & Huang, D. T.
- Affiliations
- Cancer Research UK Scotland Institute (GB)
- Corresponding author
- Huang, Danny T
- Venue
- Nature Structural & Molecular Biology
- Published
- 2012-08-14
- Volume
- 19
- Issue
- 9
- Pages
- 876-883
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- PMC
- PMC3880866
- OpenAlex
- W2001701156
- Cited by
- 319
- References
- 56
- Citations by year
- 2026: 10 · 2025: 20 · 2024: 20 · 2023: 13 · 2022: 20 · 2021: 25 · 2020: 27 · 2019: 20 · 2018: 18 · 2017: 28 · 2016: 27 · 2015: 27 · 2014: 33 · 2013: 28 · 2012: 3
- FWCI
- 11.63
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Cancer Research UK (A11593, 11593)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- BIRC7, RING E3 ubiquitin ligase, UbcH5b, ubiquitin transfer, E2 ubiquitin-conjugating enzyme, ubiquitin conjugates, protein complex structure
- MeSH terms
- Baculoviral IAP Repeat-Containing 3 Protein, Amino Acid Sequence, Humans, Models, Molecular, Molecular Sequence Data, Neoplasm Proteins, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Crystallography, X-Ray, Nuclear Magnetic Resonance, Biomolecular, Ubiquitin, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases, Adaptor Proteins, Signal Transducing, Inhibitor of Apoptosis Proteins, Ubiquitination, Protein Multimerization, Protein Interaction Maps
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