Crystal Structure of the Human Ubiquitin-activating Enzyme 5 (UBA5) Bound to ATP

@inproceedings{Bacik2010CrystalSO,
  title={Crystal Structure of the Human Ubiquitin-activating Enzyme 5 (UBA5) Bound to ATP},
  author={J Bacik and John R. Walker and M Jaffer Ali and Aaron David Schimmer and Sirano dhe-Paganon},
  booktitle={The Journal of biological chemistry},
  year={2010}
}
E1 ubiquitin-activating enzymes (UBAs) are large multidomain proteins that catalyze formation of a thioester bond between the terminal carboxylate of a ubiquitin or ubiquitin-like modifier (UBL) and a conserved cysteine in an E2 protein, producing reactive ubiquityl units for subsequent ligation to substrate lysines. Two important E1 reaction intermediates have been identified: a ubiquityl-adenylate phosphoester and a ubiquityl-enzyme thioester. However, the mechanism of thioester bond… CONTINUE READING

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