› 4lx9

X-ray diffraction
1.98Å resolution

Archaeal amino-terminal acetyltransferase (NAT) bound to acetyl coenzyme A

Released:
DOI: 10.2210/pdb4lx9/pdb
PDB entry 4lx9 coloured by chain, front view.
PDB entry 4lx9 coloured by chain, side view.
PDB entry 4lx9 coloured by chain, top view.
Source organism: Saccharolobus solfataricus P2
Primary publication:
Implications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal ortholog.
Liszczak G, Marmorstein R
Proc Natl Acad Sci U S A 110 14652-7 (2013)
PMID: 23959863

Function and Biology Details

Reactions catalysed: 
Acetyl-CoA + an N-terminal-L-alanyl-[protein] = an N-terminal-N(alpha)-acetyl-L-alanyl-[protein] + CoA
Acetyl-CoA + an N-terminal-L-methionyl-L-alanyl-[protein] = an N-terminal-N(alpha)-acetyl-L-methionyl-L-alanyl-[protein] + CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189098 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-alpha-acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 167 amino acids
Theoretical weight: 19.47 KDa
Source organism: Saccharolobus solfataricus P2
Expression system: Escherichia coli
UniProt:
  • Canonical: Q980R9 (Residues: 1-167; Coverage: 100%)
Gene names: SSO0209, ard1
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand ACO 1 x ACO
1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 100.84Å b: 35.062Å c: 51.219Å
α: 90° β: 100.05° γ: 90°
R-values:
R R work R free
0.202 0.199 0.242
Expression system: Escherichia coli

Quick links

Citations

4 review citations

N-terminal modifications of cellular proteins: The enzymes involved, their substrate specificities and biological effects.
Varland et al. (2015)
3 more

7 mentions without citation

Protein N-Terminal Acetylation: Structural Basis, Mechanism, Versatility, and Regulation.
Deng et al. (2021)
6 more