› 1i12

X-ray diffraction
1.3Å resolution

CRYSTAL STRUCTURE OF SACCHAROMYCES CEREVISIAE GNA1 COMPLEXED WITH ACCOA

Released:
DOI: 10.2210/pdb1i12/pdb
PDB entry 1i12 coloured by chain, front view.
PDB entry 1i12 coloured by chain, side view.
PDB entry 1i12 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
The crystal structures of Apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase.
Peneff C, Mengin-Lecreulx D, Bourne Y
J Biol Chem 276 16328-34 (2001)
PMID: 11278591

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155092 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucosamine 6-phosphate N-acetyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 160 amino acids
Theoretical weight: 18.26 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P43577 (Residues: 1-159; Coverage: 100%)
Gene names: GNA1, PAT1, YFL017C
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand ACO 4 x ACO
1 bound ligand:
Ligand IMD 2 x IMD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: C2
Unit cell:
a: 156.559Å b: 51.842Å c: 92.232Å
α: 90° β: 107.81° γ: 90°
R-values:
R R work R free
0.21 0.21 0.221
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

8 mentions without citation

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