› 4km3

X-ray diffraction
3.2Å resolution

Discovery of a novel structural motif in methionine aminopeptidase from Streptococci with possible post-translational modification

Released:
DOI: 10.2210/pdb4km3/pdb
PDB entry 4km3 coloured by chain, front view.
PDB entry 4km3 coloured by chain, side view.
PDB entry 4km3 coloured by chain, top view.
Source organism: Streptococcus pneumoniae CGSP14
Primary publication:
Discovery of a new genetic variant of methionine aminopeptidase from Streptococci with possible post-translational modifications: biochemical and structural characterization.
Arya T, Kishor C, Saddanapu V, Reddi R, Addlagatta A
PLoS One 8 e75207 (2013)
PMID: 24124477

Function and Biology Details

Reaction catalysed: 
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109610 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine aminopeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 286 amino acids
Theoretical weight: 31.7 KDa
Source organism: Streptococcus pneumoniae CGSP14
Expression system: Escherichia coli
UniProt:
  • Canonical: B2IQ22 (Residues: 1-286; Coverage: 100%)
Gene names: SPCG_1194, map
Sequence domains: Metallopeptidase family M24
Structure domains: Creatinase/methionine aminopeptidase superfamily

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P65
Unit cell:
a: 109.687Å b: 109.687Å c: 164.424Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.214 0.21 0.285
Expression system: Escherichia coli

Quick links

Citations

2 review citations

N-terminal protein modifications: Bringing back into play the ribosome.
Giglione et al. (2015)
1 more

3 mentions without citation

A mutation in the methionine aminopeptidase gene provides phage resistance in Streptococcus thermophilus.
Labrie et al. (2019)
2 more