› 2cnt

X-ray diffraction
2.4Å resolution

RimI - Ribosomal S18 N-alpha-protein acetyltransferase in complex with CoenzymeA.

Released:
DOI: 10.2210/pdb2cnt/pdb
PDB entry 2cnt coloured by chain, front view.
PDB entry 2cnt coloured by chain, side view.
PDB entry 2cnt coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Primary publication:
Crystal structure of RimI from Salmonella typhimurium LT2, the GNAT responsible for N(alpha)-acetylation of ribosomal protein S18.
Vetting MW, Bareich DC, Yu M, Blanchard JS
Protein Sci 17 1781-90 (2008)
PMID: 18596200

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + an N-terminal L-alanyl-[S18 protein of 30S ribosome] = CoA + an N-terminal N-acetyl-L-alanyl-[S18 protein of 30S ribosome]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187218 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
[Ribosomal protein bS18]-alanine N-acetyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 160 amino acids
Theoretical weight: 18.33 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8ZJW4 (Residues: 1-148; Coverage: 100%)
Gene names: STM4558, rimI
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments

3 bound ligands:
Ligand COA 4 x COA
Ligand GOL 4 x GOL
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200B
Spacegroup: P321
Unit cell:
a: 126.926Å b: 126.926Å c: 113.859Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.186 0.223
Expression system: Escherichia coli

Quick links

Citations

9 review citations

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

7 mentions without citation

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