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- W3009576495 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." @default.
- W3009576495 created "2020-03-13" @default.
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- W3009576495 date "2020-02-28" @default.
- W3009576495 modified "2023-10-03" @default.
- W3009576495 title "High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation" @default.
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- W3009576495 doi "https://doi.org/10.1038/s41467-020-14847-3" @default.
- W3009576495 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7048800" @default.
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