Nature Communications (Aug 2021)

Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD

  • Luke A. Perera,
  • Steffen Preissler,
  • Nathan R. Zaccai,
  • Sylvain Prévost,
  • Juliette M. Devos,
  • Michael Haertlein,
  • David Ron

DOI
https://doi.org/10.1038/s41467-021-25076-7
Journal volume & issue
Vol. 12, no. 1
pp. 1 – 18

Abstract

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The ER chaperone BiP is regulated by FICD-mediated AMPylation and deAMPylation. Here, the authors characterise the structure of mammalian AMPylated BiP bound to FICD, by X-ray crystallography and neutron scattering, providing insights into the mechanism of BiP AMPylation and deAMPylation.