3RTR

A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases

Summary for 3RTR

• Entry DOI: 10.2210/pdb3rtr/pdb
• Descriptor: Cullin-1, E3 ubiquitin-protein ligase RBX1, ZINC ION (3 entities in total)
• Functional Keywords: ubiquitin, nedd8, cullin, ubl conjugation pathway, e3 ligase, ligase
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P62877
• Total number of polymer chains: 8
• Total formula weight: 219919.76

Authors

Calabrese, M.F.,Scott, D.C.,Duda, D.M.,Grace, C.R.,Kurinov, I.,Kriwacki, R.W.,Schulman, B.A. (deposition date: 2011-05-03, release date: 2011-07-20, Last modification date: 2023-09-13)

Primary citation

Calabrese, M.F.,Scott, D.C.,Duda, D.M.,Grace, C.R.,Kurinov, I.,Kriwacki, R.W.,Schulman, B.A.
A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases.
Nat.Struct.Mol.Biol., 18:947-949, 2011

PubMed Abstract: 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.

PubMed: 21765416
DOI: 10.1038/nsmb.2086

Experimental method

X-RAY DIFFRACTION (3.21 Å)