› 6nas

X-ray diffraction
2.9Å resolution

Ternary Complex of Ac-Alpha-Actin with Profilin and AcCoA-NAA80

Released:
DOI: 10.2210/pdb6nas/pdb
PDB entry 6nas coloured by chain, front view.
PDB entry 6nas coloured by chain, side view.
PDB entry 6nas coloured by chain, top view.
Source organisms:
Primary publication:
Mechanism of actin N-terminal acetylation.
Rebowski G, Boczkowska M, Drazic A, Ree R, Goris M, Arnesen T, Dominguez R
Sci Adv 6 eaay8793 (2020)
PMID: 32284999

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-139730 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Actin, alpha skeletal muscle Chain: A
Molecule details ›
Chain: A
Length: 375 amino acids
Theoretical weight: 41.92 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P68135 (Residues: 3-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin
N-alpha-acetyltransferase 80 Chain: N
Molecule details ›
Chain: N
Length: 235 amino acids
Theoretical weight: 25.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q93015 (Residues: 56-286; Coverage: 81%)
Gene names: FUS2, NAA80, NAT6
Sequence domains: Acetyltransferase (GNAT) family
Profilin-1 Chain: P
Molecule details ›
Chain: P
Length: 140 amino acids
Theoretical weight: 15.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07737 (Residues: 1-140; Coverage: 100%)
Gene name: PFN1
Sequence domains: Profilin

Ligands and Environments

6 bound ligands:
Ligand CA 1 x CA
Ligand ATP 1 x ATP
Ligand LAB 1 x LAB
Ligand GOL 3 x GOL
Ligand ACO 1 x ACO
Ligand MES 1 x MES
2 modified residues:
Ligand KKD 1 x KKD
Ligand HIC 1 x HIC

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: C2221
Unit cell:
a: 103.83Å b: 114.89Å c: 132.271Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.184 0.239
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

4 mentions without citation

Mechanism of actin N-terminal acetylation.
Rebowski et al. (2020)
3 more