Cited by 523Ubiquitin and proteasome pathwaysEnzyme Structure and FunctionProtein Degradation and Inhibitors

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Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis

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Plechanovová, Anna, Jaffray, Ellis G., Tatham, Michael H., Naismith, James H., Hay, Ronald T.·2012·Nature

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Abstract

Ubiquitin modification is mediated by a large family of specificity determining ubiquitin E3 ligases. To facilitate ubiquitin transfer, RING E3 ligases bind both substrate and a ubiquitin E2 conjugating enzyme linked to ubiquitin via a thioester bond, but the mechanism of transfer has remained elusive. Here we report the crystal structure of the dimeric RING domain of rat RNF4 in complex with E2 (UbcH5A) linked by an isopeptide bond to ubiquitin. While the E2 contacts a single protomer of the RING, ubiquitin is folded back onto the E2 by contacts from both RING protomers. The carboxy-terminal tail of ubiquitin is locked into an active site groove on the E2 by an intricate network of interactions, resulting in changes at the E2 active site. This arrangement is primed for catalysis as it can deprotonate the incoming substrate lysine residue and stabilize the consequent tetrahedral transition-state intermediate.

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Authors: Plechanovová, A., Jaffray, E. G., Tatham, M. H., Naismith, J. H., & Hay, R. T.
Affiliations: University of Dundee (GB)
University of St Andrews (GB)
Corresponding author: Hay, Ronald T.
ORCID: Plechanovová, Anna
Jaffray, Ellis G.
Tatham, Michael H.
Naismith, James H.
Hay, Ronald T.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2012-07-29
Volume: 489
Issue: 7414
Pages: 115-120
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature11376
PMC: PMC3442243
OpenAlex: W2147542927
Cited by: 521
References: 41
Citations by year: 2026: 25 · 2025: 36 · 2024: 41 · 2023: 24 · 2022: 41 · 2021: 39 · 2020: 41 · 2019: 29 · 2018: 27 · 2017: 44 · 2016: 39 · 2015: 37 · 2014: 47 · 2013: 46 · 2012: 5
FWCI: 17.37
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Discovery Research Portal (University of Dundee) (submittedVersion)
Funders: Wellcome Trust (098391, 081862, 098391/Z/12/Z)
Cancer Research UK (13067)
Scottish Funding Council
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
Keywords: RING E3 ubiquitin ligase, RNF4, UbcH5a, ubiquitin transfer, isopeptide bonds, ubiquitin binding, crystal structure
MeSH terms: Animals, Humans, Hydrolysis, Models, Molecular, Mutation, Nuclear Proteins, Protein Binding, Transcription Factors, Zinc Fingers, Protein Structure, Tertiary, Crystallography, X-Ray, Catalytic Domain, Ubiquitin, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases, Multiprotein Complexes, Rats, Ubiquitination, Biocatalysis

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Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis

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