BibTex format
@article{Dian:2020:10.1038/s41467-020-14847-3,
author = {Dian, C and Inmaculada, P-D and Riviere, F and Asensio, T and Legrand, P and Ritzefeld, M and Shen, M and Cota, E and Meinnel, T and Tate, E and Giglione, C},
doi = {10.1038/s41467-020-14847-3},
journal = {Nature Communications},
pages = {1--15},
title = {High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation},
url = {http://dx.doi.org/10.1038/s41467-020-14847-3},
volume = {11},
year = {2020}
}
RIS format (EndNote, RefMan)
TY - JOUR
AB - 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.
AU - Dian,C
AU - Inmaculada,P-D
AU - Riviere,F
AU - Asensio,T
AU - Legrand,P
AU - Ritzefeld,M
AU - Shen,M
AU - Cota,E
AU - Meinnel,T
AU - Tate,E
AU - Giglione,C
DO - 10.1038/s41467-020-14847-3
EP - 15
PY - 2020///
SN - 2041-1723
SP - 1
TI - High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation
T2 - Nature Communications
UR - http://dx.doi.org/10.1038/s41467-020-14847-3
UR - https://www.nature.com/articles/s41467-020-14847-3
UR - http://hdl.handle.net/10044/1/77568
VL - 11
ER -
