› 2p6g

X-ray diffraction
3Å resolution

Crystal structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoyl-CoA and inhibitors

Released:
DOI: 10.2210/pdb2p6g/pdb
PDB entry 2p6g coloured by chain, front view.
PDB entry 2p6g coloured by chain, side view.
PDB entry 2p6g coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Crystal structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoyl-CoA and inhibitors reveal the functional roles of the N-terminal region.
Wu J, Tao Y, Zhang M, Howard MH, Gutteridge S, Ding J
J Biol Chem 282 22185-94 (2007)
PMID: 17513302

Function and Biology Details

Reaction catalysed: 
Tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147064 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycylpeptide N-tetradecanoyltransferase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 455 amino acids
Theoretical weight: 52.91 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P14743 (Residues: 1-455; Coverage: 100%)
Gene names: CDC72, L8167.14, NMT1, YLR195C
Sequence domains:
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand MYA 6 x MYA
1 bound ligand:
Ligand 3LP 2 x 3LP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 188.847Å b: 151.301Å c: 134.195Å
α: 90° β: 107.64° γ: 90°
R-values:
R R work R free
0.263 0.26 0.318
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Global profiling of protein lipidation using chemical proteomic technologies.
Tate et al. (2015)
3 more

5 mentions without citation

Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).
Salah Ud-Din et al. (2016)
4 more