› 2nmt

X-ray diffraction
2.9Å resolution

MYRISTOYL-COA:PROTEIN N-MYRISTOYLTRANSFERASE BOUND TO MYRISTOYL-COA AND PEPTIDE ANALOGS

Released:
DOI: 10.2210/pdb2nmt/pdb
PDB entry 2nmt coloured by chain, front view.
PDB entry 2nmt coloured by chain, side view.
PDB entry 2nmt coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structure of N-myristoyltransferase with bound myristoylCoA and peptide substrate analogs.
Bhatnagar RS, Fütterer K, Farazi TA, Korolev S, Murray CL, Jackson-Machelski E, Gokel GW, Gordon JI, Waksman G
Nat Struct Biol 5 1091-7 (1998)
PMID: 9846880

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 domain:

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 Chain: A
Molecule details ›
Chain: A
Length: 422 amino acids
Theoretical weight: 49.01 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P14743 (Residues: 34-455; Coverage: 93%)
Gene names: CDC72, L8167.14, NMT1, YLR195C
Sequence domains:
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand NHM 1 x NHM
2 bound ligands:
Ligand MIM 1 x MIM
Ligand GOL 12 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P3121
Unit cell:
a: 105.4Å b: 105.4Å c: 106.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.228 0.228 0.297
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins.
Resh MD. (1999)
19 more

7 mentions without citation

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