› 1s7n

X-ray diffraction
2.1Å resolution

Ribosomal L7/L12 alpha-N-protein acetyltransferase in complex with Coenzyme A (CoA free sulfhydryl)

Released:
DOI: 10.2210/pdb1s7n/pdb
PDB entry 1s7n coloured by chain, front view.
PDB entry 1s7n coloured by chain, side view.
PDB entry 1s7n coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Primary publication:
A novel dimeric structure of the RimL Nalpha-acetyltransferase from Salmonella typhimurium.
Vetting MW, de Carvalho LP, Roderick SL, Blanchard JS
J Biol Chem 280 22108-14 (2005)
PMID: 15817456

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187326 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyltransferase domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 182 amino acids
Theoretical weight: 20.91 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8ZPC0 (Residues: 1-179; Coverage: 100%)
Gene names: STM1611, rimL
Sequence domains: Acetyltransferase (GNAT) domain
Structure domains: Aminopeptidase

Ligands and Environments

1 bound ligand:
Ligand COA 4 x COA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 54.3Å b: 82.3Å c: 95.5Å
α: 90° β: 94.8° γ: 90°
R-values:
R R work R free
0.18 0.18 0.231
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Beyond gene expression: the impact of protein post-translational modifications in bacteria.
Cain et al. (2014)
3 more

10 mentions without citation

Bacterial GCN5-Related N-Acetyltransferases: From Resistance to Regulation.
Favrot et al. (2016)
9 more