Structural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34
Abstract
Ubiquitin (Ub) signaling requires the sequential interactions and activities of three enzymes, E1, E2, and E3. Cdc34 is an E2 that plays a key role in regulating cell cycle progression and requires unique structural elements to function. The molecular basis by which Cdc34 engages its E1 and the structural mechanisms by which its unique C-terminal extension functions in Cdc34 activity are unknown. Here, we present crystal structures of Cdc34 alone and in complex with E1, and a Cdc34~Ub thioester mimetic that represents the product of Uba1-Cdc34 Ub transthiolation. These structures reveal conformational changes in Uba1 and Cdc34 and a unique binding mode that are required for transthiolation. The Cdc34~Ub structure reveals contacts between the Cdc34 C-terminal extension and Ub that stabilize Cdc34~Ub in a closed conformation and are critical for Ub discharge. Altogether, our structural, biochemical, and cell-based studies provide insights into the molecular mechanisms by which Cdc34 function in cells.
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Org.:
- USDOE Office of Science (SC); National Institutes of Health (NIH); Abney Foundation
- OSTI Identifier:
- 1557318
- Grant/Contract Number:
- AC02-06CH11357; S10 RR029205; S10 RR027139-01; NIH R01 GM115568; R01 GM128731; NIH P01 CA098101; R01 CA093237; NIH F30 CA216921; NIH T32 CA193201; NIH T32 DE017551
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nature Communications
- Additional Journal Information:
- Journal Volume: 10; Journal Issue: 1; Journal ID: ISSN 2041-1723
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; cell division; enzyme mechanisms; ubiquitylation; x-ray crystallography
Citation Formats
Williams, Katelyn M., Qie, Shuo, Atkison, James H., Salazar-Arango, Sabrina, Alan Diehl, J., and Olsen, Shaun K. Structural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34. United States: N. p., 2019.
Web. doi:10.1038/s41467-019-11061-8.
Williams, Katelyn M., Qie, Shuo, Atkison, James H., Salazar-Arango, Sabrina, Alan Diehl, J., & Olsen, Shaun K. Structural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34. United States. https://doi.org/10.1038/s41467-019-11061-8
Williams, Katelyn M., Qie, Shuo, Atkison, James H., Salazar-Arango, Sabrina, Alan Diehl, J., and Olsen, Shaun K. Wed .
"Structural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34". United States. https://doi.org/10.1038/s41467-019-11061-8. https://www.osti.gov/servlets/purl/1557318.
@article{osti_1557318,
title = {Structural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34},
author = {Williams, Katelyn M. and Qie, Shuo and Atkison, James H. and Salazar-Arango, Sabrina and Alan Diehl, J. and Olsen, Shaun K.},
abstractNote = {Ubiquitin (Ub) signaling requires the sequential interactions and activities of three enzymes, E1, E2, and E3. Cdc34 is an E2 that plays a key role in regulating cell cycle progression and requires unique structural elements to function. The molecular basis by which Cdc34 engages its E1 and the structural mechanisms by which its unique C-terminal extension functions in Cdc34 activity are unknown. Here, we present crystal structures of Cdc34 alone and in complex with E1, and a Cdc34~Ub thioester mimetic that represents the product of Uba1-Cdc34 Ub transthiolation. These structures reveal conformational changes in Uba1 and Cdc34 and a unique binding mode that are required for transthiolation. The Cdc34~Ub structure reveals contacts between the Cdc34 C-terminal extension and Ub that stabilize Cdc34~Ub in a closed conformation and are critical for Ub discharge. Altogether, our structural, biochemical, and cell-based studies provide insights into the molecular mechanisms by which Cdc34 function in cells.},
doi = {10.1038/s41467-019-11061-8},
journal = {Nature Communications},
number = 1,
volume = 10,
place = {United States},
year = {Wed Jul 24 00:00:00 EDT 2019},
month = {Wed Jul 24 00:00:00 EDT 2019}
}
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