› 6vfm

X-ray diffraction
2.67Å resolution

Crystal structure of SpeG allosteric polyamine acetyltransferase from Bacillus thuringiensis

Released:
DOI: 10.2210/pdb6vfm/pdb
PDB entry 6vfm coloured by chain, front view.
PDB entry 6vfm coloured by chain, side view.
PDB entry 6vfm coloured by chain, top view.
Source organism: Bacillus thuringiensis serovar finitimus YBT-020
Primary publication:
SpeG polyamine acetyltransferase enzyme from Bacillus thuringiensis forms a dodecameric structure and exhibits high catalytic efficiency.
Tsimbalyuk S, Shornikov A, Thi Bich Le V, Kuhn ML, Forwood JK
J Struct Biol 210 107506 (2020)
PMID: 32283314

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-105042 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GNAT family N-acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 171 amino acids
Theoretical weight: 20.65 KDa
Source organism: Bacillus thuringiensis serovar finitimus YBT-020
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A437SL45 (Residues: 1-171; Coverage: 100%)
Gene name: BM74_11955
Sequence domains: Acetyltransferase (GNAT) domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P6322
Unit cell:
a: 159.374Å b: 159.374Å c: 106.205Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.275 0.274 0.293
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Structural characterization of a GNAT family acetyltransferase from Elizabethkingia anophelis bound to acetyl-CoA reveals a new dimeric interface.
Shirmast et al. (2021)
4 more

1 mention without citation

SpeG polyamine acetyltransferase enzyme from Bacillus thuringiensis forms a dodecameric structure and exhibits high catalytic efficiency.
Tsimbalyuk et al. (2020)