Nature Communications (Feb 2020)

High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation

  • Cyril Dian,
  • Inmaculada Pérez-Dorado,
  • Frédéric Rivière,
  • Thomas Asensio,
  • Pierre Legrand,
  • Markus Ritzefeld,
  • Mengjie Shen,
  • Ernesto Cota,
  • Thierry Meinnel,
  • Edward W. Tate,
  • Carmela Giglione

DOI
https://doi.org/10.1038/s41467-020-14847-3
Journal volume & issue
Vol. 11, no. 1
pp. 1 – 15

Abstract

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N-terminal glycine myristoyl transferases (NMTs) catalyse the myristoylation of eukaryotic proteins. Here, the authors provide insights into the catalytic mechanism of NMTs by determining the crystal structures of human NMT1 in complex with reactive cognate lipid and peptide substrates and further show that NMT1 also catalyses the acylation of N-terminal lysines.