Nature Communications (Aug 2022)
Crystal structures reveal catalytic and regulatory mechanisms of the dual-specificity ubiquitin/FAT10 E1 enzyme Uba6
- Lingmin Yuan,
- Fei Gao,
- Zongyang Lv,
- Digant Nayak,
- Anindita Nayak,
- Priscila dos Santos Bury,
- Kristin E. Cano,
- Lijia Jia,
- Natalia Oleinik,
- Firdevs Cansu Atilgan,
- Besim Ogretmen,
- Katelyn M. Williams,
- Christopher Davies,
- Farid El Oualid,
- Elizabeth V. Wasmuth,
- Shaun K. Olsen
Affiliations
- Lingmin Yuan
- Department of Biochemistry & Structural Biology, University of Texas Health Science Center at San Antonio
- Fei Gao
- Department of Biochemistry & Structural Biology, University of Texas Health Science Center at San Antonio
- Zongyang Lv
- Department of Biochemistry & Structural Biology, University of Texas Health Science Center at San Antonio
- Digant Nayak
- Department of Biochemistry & Structural Biology, University of Texas Health Science Center at San Antonio
- Anindita Nayak
- Department of Biochemistry & Structural Biology, University of Texas Health Science Center at San Antonio
- Priscila dos Santos Bury
- Department of Biochemistry & Structural Biology, University of Texas Health Science Center at San Antonio
- Kristin E. Cano
- Department of Biochemistry & Structural Biology, University of Texas Health Science Center at San Antonio
- Lijia Jia
- Department of Biochemistry & Structural Biology, University of Texas Health Science Center at San Antonio
- Natalia Oleinik
- Department of Biochemistry & Molecular Biology and Hollings Cancer Center, Medical University of South Carolina
- Firdevs Cansu Atilgan
- Department of Biochemistry & Molecular Biology and Hollings Cancer Center, Medical University of South Carolina
- Besim Ogretmen
- Department of Biochemistry & Molecular Biology and Hollings Cancer Center, Medical University of South Carolina
- Katelyn M. Williams
- Department of Pediatrics, Johns Hopkins University School of Medicine
- Christopher Davies
- Department of Biochemistry & Molecular Biology, University of South Alabama
- Farid El Oualid
- UbiQ Bio B.V.
- Elizabeth V. Wasmuth
- Department of Biochemistry & Structural Biology, University of Texas Health Science Center at San Antonio
- Shaun K. Olsen
- Department of Biochemistry & Structural Biology, University of Texas Health Science Center at San Antonio
- DOI
- https://doi.org/10.1038/s41467-022-32613-5
- Journal volume & issue
-
Vol. 13,
no. 1
pp. 1 – 14
Abstract
Uba6 is an E1 enzyme that regulates numerous cellular processes by activating ubiquitin and FAT10 pathways. Here, the authors present crystal structures that illuminate Uba6 catalytic mechanisms and reveal inositol hexakisphosphate as a cofactor that modulates Uba6 activity.
