4C2Y: Human N-myristoyltransferase (nmt1) With Myristoyl-coa Co-factor

Citation:
Abstract
Protein N-myristoylation is a ubiquitous co- and post-translational modification that has been implicated in the development and progression of a range of human diseases. Here, we report the global N-myristoylated proteome in human cells determined using quantitative chemical proteomics combined with potent and specific human N-myristoyltransferase (NMT) inhibition. Global quantification of N-myristoylation during normal growth or apoptosis allowed the identification of >100 N-myristoylated proteins, >95% of which are identified for the first time at endogenous levels. Furthermore, quantitative dose response for inhibition of N-myristoylation is determined for >70 substrates simultaneously across the proteome. Small-molecule inhibition through a conserved substrate-binding pocket is also demonstrated by solving the crystal structures of inhibitor-bound NMT1 and NMT2. The presented data substantially expand the known repertoire of co- and post-translational N-myristoylation in addition to validating tools for the pharmacological inhibition of NMT in living cells.
PDB ID: 4C2YDownload
MMDB ID: 123520
PDB Deposition Date: 2013/8/20
Updated in MMDB: 2014/10
Experimental Method:
x-ray diffraction
Resolution: 1.64  Å
Source Organism:
Similar Structures:
Biological Unit for 4C2Y: monomeric; determined by author and by software (PISA)
Molecular Components in 4C2Y
Label Count Molecule
Protein (1 molecule)
1
Glycylpeptide N-tetradecanoyltransferase 1(Gene symbol: NMT1)
Molecule annotation
Chemicals (7 molecules)
1
1
2
1
3
1
4
4
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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