› 1iid

X-ray diffraction
2.5Å resolution

Crystal Structure of Saccharomyces cerevisiae N-myristoyltransferase with Bound S-(2-oxo)pentadecylCoA and the Octapeptide GLYASKLA

Released:
DOI: 10.2210/pdb1iid/pdb
PDB entry 1iid coloured by chain, front view.
PDB entry 1iid coloured by chain, side view.
PDB entry 1iid coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoylCoA and peptide provide insights about substrate recognition and catalysis.
Farazi TA, Waksman G, Gordon JI
Biochemistry 40 6335-43 (2001)
PMID: 11371195

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147065 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
Octapeptide GLYASKLA Chain: O
Molecule details ›
Chain: O
Length: 8 amino acids
Theoretical weight: 823 Da
Source organism: Saccharomyces cerevisiae
Expression system: Not provided

Ligands and Environments


Cofactor: Ligand NHM 1 x NHM
1 bound ligand:
Ligand NI 2 x NI
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 75.129Å b: 97.06Å c: 141.809Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.242 0.288
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

8 review citations

Structure and functions of the GNAT superfamily of acetyltransferases.
Vetting et al. (2005)
7 more

12 mentions without citation

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