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Citation

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}
}
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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  -
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Contact

Prof. Ed Tate
GSK Chair in Chemical Biology
Department of Chemistry
Molecular Sciences Research Hub, White City Campus,
82 Wood Lane, London, W12 0BZ

e.tate@imperial.ac.uk
Tel: +44 (0)20 759 + ext 43752 or 45821