› 5wje

X-ray diffraction
1.76Å resolution

Crystal structure of Naa80 bound to a bisubstrate analogue

Released:
DOI: 10.2210/pdb5wje/pdb
PDB entry 5wje coloured by chain, front view.
PDB entry 5wje coloured by chain, side view.
PDB entry 5wje coloured by chain, top view.
Source organism: Drosophila melanogaster
Primary publication:
Structural determinants and cellular environment define processed actin as the sole substrate of the N-terminal acetyltransferase NAA80.
Goris M, Magin RS, Foyn H, Myklebust LM, Varland S, Ree R, Drazic A, Bhambra P, Støve SI, Baumann M, Haug BE, Marmorstein R, Arnesen T
Proc Natl Acad Sci U S A 115 4405-4410 (2018)
PMID: 29581307

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-166268 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
N-alpha-acetyltransferase 80 Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 18.13 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
  • Canonical: Q59DX8 (Residues: 20-178; Coverage: 89%)
Gene names: CG8481, Naa80
Sequence domains: Acetyltransferase (GNAT) family
Actin N-terminus peptide Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 474 Da
Source organism: Drosophila melanogaster
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand CMC 1 x CMC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P212121
Unit cell:
a: 37.136Å b: 64.37Å c: 68.589Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.177 0.218
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

5 review citations

Co-translational, Post-translational, and Non-catalytic Roles of N-Terminal Acetyltransferases.
Aksnes et al. (2019)
4 more

5 mentions without citation

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