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I03-Macromolecular Crystallography	High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation Cyril Dian , Inmaculada Perez-Dorado , Frédéric Rivière , Thomas Asensio , Pierre Legrand , Markus Ritzefeld , Mengjie Shen , Ernesto Cota , Thierry Meinnel , Edward Tate , Carmela Giglione Nature Communications 11 DOI: 10.1038/s41467-020-14847-3 Diamond Proposal Number(s): [12579] Open Access Show Abstract ▼ Abstract: The promising drug target N-myristoyltransferase (NMT) catalyses an essential protein modification thought to occur exclusively at N-terminal glycines (Gly). Here, we present high-resolution human NMT1 structures co-crystallised with reactive cognate lipid and peptide substrates, revealing high-resolution snapshots of the entire catalytic mechanism from the initial to final reaction states. Structural comparisons, together with biochemical analysis, provide unforeseen details about how NMT1 reaches a catalytically competent conformation in which the reactive groups are brought into close proximity to enable catalysis. We demonstrate that this mechanism further supports efficient and unprecedented myristoylation of an N-terminal lysine side chain, providing evidence that NMT acts both as N-terminal-lysine and glycine myristoyltransferase.	Feb 2020

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