Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1.

@article{Lois2005StructuresOT,
  title={Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1.},
  author={Luisa Mar{\'i}a Lois and Christopher D Lima},
  journal={The EMBO journal},
  year={2005},
  volume={24 3},
  pages={439-51}
}
E1 enzymes facilitate conjugation of ubiquitin and ubiquitin-like proteins through adenylation, thioester transfer within E1, and thioester transfer from E1 to E2 conjugating proteins. Structures of human heterodimeric Sae1/Sae2-Mg.ATP and Sae1/Sae2-SUMO-1-Mg.ATP complexes were determined at 2.2 and 2.75 A resolution, respectively. Despite the presence of Mg.ATP, the Sae1/Sae2-SUMO-1-Mg.ATP structure reveals a substrate complex insomuch as the SUMO C-terminus remains unmodified within the… CONTINUE READING
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