Nature Communications (Apr 2020)

Structural insights into the mechanism and inhibition of transglutaminase-induced ubiquitination by the Legionella effector MavC

  • Yajuan Mu,
  • Yue Wang,
  • Yanfei Huang,
  • Dong Li,
  • Youyou Han,
  • Min Chang,
  • Jiaqi Fu,
  • Yongchao Xie,
  • Jie Ren,
  • Hao Wang,
  • Yi Zhang,
  • Zhao-Qing Luo,
  • Yue Feng

DOI
https://doi.org/10.1038/s41467-020-15645-7
Journal volume & issue
Vol. 11, no. 1
pp. 1 – 13

Abstract

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The Legionella effector MavC catalyses the ubiquitination of the E2 enzyme UBE2N in the host cell through a transglutamination reaction, which can be inhibited by the Legionella effector Lpg2149. Here, the authors provide mechanistic insights into these processes by determining the crystal structures of the MavC/UBE2N/Ub ternary complex, the MavC/UBE2N-Ub product complex and the MavC/Lpg2149 complex.