› 4r3k

X-ray diffraction
2.13Å resolution

Crystal structure of Ard1 N-terminal acetyltransferase from Sulfolobus solfataricus bound to CoA

Released:
DOI: 10.2210/pdb4r3k/pdb
PDB entry 4r3k coloured by chain, front view.
PDB entry 4r3k coloured by chain, side view.
PDB entry 4r3k coloured by chain, top view.
Source organism: Saccharolobus solfataricus P2
Primary publication:
Structural basis for substrate-specific acetylation of Nα-acetyltransferase Ard1 from Sulfolobus solfataricus.
Chang YY, Hsu CH
Sci Rep 5 8673 (2015)
PMID: 25728374

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: 173 amino acids
Theoretical weight: 20.3 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 COA 1 x COA
2 bound ligands:
Ligand SO4 2 x SO4
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P212121
Unit cell:
a: 35.353Å b: 58.224Å c: 85.265Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.172 0.217
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The biological functions of Naa10 - From amino-terminal acetylation to human disease.
Dörfel et al. (2015)
1 more

2 mentions without citation

Structural basis for substrate-specific acetylation of Nα-acetyltransferase Ard1 from Sulfolobus solfataricus.
Chang et al. (2015)
1 more