4C2X

Human N-myristoyltransferase isoform 2 (NMT2)

Summary for 4C2X

• Entry DOI: 10.2210/pdb4c2x/pdb
• Related: 4C2Y 4C2Z
• Descriptor: GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE 2, MAGNESIUM ION, 2-oxopentadecyl-CoA, ... (4 entities in total)
• Functional Keywords: transferase, myristoylation
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm: O60551
• Total number of polymer chains: 1
• Total formula weight: 48606.92

Authors

Thinon, E.,Serwa, R.A.,Brannigan, J.A.,Brassat, U.,Wright, M.H.,Heal, W.P.,Wilkinson, A.J.,Mann, D.J.,Tate, E.W. (deposition date: 2013-08-20, release date: 2014-10-01, Last modification date: 2023-12-20)

Primary citation

Thinon, E.,Serwa, R.A.,Broncel, M.,Brannigan, J.A.,Brassat, U.,Wright, M.H.,Heal, W.P.,Wilkinson, A.J.,Mann, D.J.,Tate, E.W.
Global Profiling of Co- and Post-Translationally N-Myristoylated Proteomes in Human Cells.
Nat.Commun., 5:4919-, 2014

PubMed 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.

PubMed: 25255805
DOI: 10.1038/NCOMMS5919

Experimental method

X-RAY DIFFRACTION (2.33 Å)