Extended Data Fig. 4: Conformational rearrangement of neddylated CUL9-RBX1. | Nature Structural & Molecular Biology

Extended Data Fig. 4: Conformational rearrangement of neddylated CUL9-RBX1.

From: Noncanonical assembly, neddylation and chimeric cullin–RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex

Extended Data Fig. 4

a, Model of the neddylation structure of CUL1 (PDB: 4P5O, with the E2 UBE2M representing similarly structured UBE2F, and DCN1 hidden) aligned with unneddylated CUL9-RBX1 protomer over RBX1 RING domain. b, Neddylated (colored) and unneddylated (grey) conformations of CUL9-RBX1 aligned on C/R domain. 35° reorientation of WHB domain highlighted with orange arrow. c, After aligning neddylated and unneddylated CUL9-RBX1 over their C/R domains, the WHB domain of unneddylated CUL9-RBX1 (grey) is shown superimposed on neddylated CUL9-RBX1 (colored). The WHB domain from neddylated CUL9 must rearrange due to steric clashing with its Ariadne domain. d, RBX1 RING domain reorientation in neddylated (colored) versus unneddylated (grey) CUL9-RBX1. RBX1 RING domain is rotated by 160˚, indicated by orange arrow. e, Comparison between binding of the Ariadne domain in the CUL1-ARIH1 E3–E3 super-assembly (PDB: 7B5L, CUL1, SKP1, SKP2, p27, CKSHS1, CDK2, Cyclin A, NEDD8, ubiquitin and UBE2L3 not shown) versus CUL9’s intrinsic Ariadne domain and collaborating RBX1. Structures are aligned on the Ariadne domain.

Back to article page