Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA.
Nat Struct Mol Biol. 2011 Jul 17;18(8):947-9. doi: 10.1038/nsmb.2086.
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.
RING E3 连接酶如何介导 E2 到底物泛素样蛋白 (UBL) 的转移尚不清楚。在这里，我们研究了 RING E3 RBX1 如何定位 NEDD8 的 E2（UBC12）和底物（CUL1）。我们发现现有的结构与 CUL1 NEDD8 化不兼容，并报告了 RBX1 的一种新构象，使 UBC12 与 CUL1 相邻。我们提出 RING 结构域旋转是 E3 中最大家族 UBL 转移的一般机制。
