A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases.
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.
Mesh Terms:
Carrier Proteins, Cullin Proteins, Models, Molecular, Mutagenesis, Site-Directed, Protein Structure, Tertiary, S-Phase Kinase-Associated Proteins, SKP Cullin F-Box Protein Ligases, Saccharomyces cerevisiae Proteins, Transcription Factors, Ubiquitin-Conjugating Enzymes, Ubiquitins
Carrier Proteins, Cullin Proteins, Models, Molecular, Mutagenesis, Site-Directed, Protein Structure, Tertiary, S-Phase Kinase-Associated Proteins, SKP Cullin F-Box Protein Ligases, Saccharomyces cerevisiae Proteins, Transcription Factors, Ubiquitin-Conjugating Enzymes, Ubiquitins
Nat. Struct. Mol. Biol.
Date: Aug. 01, 2011
PubMed ID: 21765416
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