How RING E3 ligases mediate E2-to-substrate ubiquitin-like protein (UBL) transfer remains unknown. Here we address how the RING E3 RBX1 positions NEDD8's E2 (UBC12) and substrate (CUL1). We find that existing structures are incompatible with CUL1 NEDD8ylation and report a new conformation of RBX1 that places UBC12 adjacent to CUL1. We propose RING domain rotation as a general mechanism for UBL transfer for the largest family of E3s.
A RING E3–substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases
M. Calabrese,D. C. Scott,David M. Duda,C. Grace,I. Kurinov,R. Kriwacki,B. Schulman
Published 2011 in Nature Structural &Molecular Biology
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- Publication year
2011
- Venue
Nature Structural &Molecular Biology
- Publication date
2011-07-17
- Fields of study
Biology, Medicine, Chemistry
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- Source metadata
Semantic Scholar, PubMed
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