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Bernhard C Lechtenberg, Akhil Rajput, Ruslan Sanishvili, Małgorzata K Dobaczewska, Carl F Ware, Peter D Mace, and Stefan J Riedl., Nature, 2016
Modification of protein substrates with ubiquitin affects many aspects of cellular signalling and function. Until recently, two types of ubiquitin E3 ligases were known to attach ubiquitin to substrate proteins. RBR ubiquitin E3 ligases are a recently discovered class of E3 that have features of the two previously known types of ubiquitin ligase. This work reports the first structure of the fully active HOIP RBR in its transfer complex with an E2~ubiquitin conjugate and shows how the active conformation aligns the E2 and E3 catalytic centres for ubiquitin transfer.