› 1mat

X-ray diffraction
2.4Å resolution

STRUCTURE OF THE COBALT-DEPENDENT METHIONINE AMINOPEPTIDASE FROM ESCHERICHIA COLI: A NEW TYPE OF PROTEOLYTIC ENZYME

Released:
DOI: 10.2210/pdb1mat/pdb
PDB entry 1mat coloured by chain, front view.
PDB entry 1mat coloured by chain, side view.
PDB entry 1mat coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme.
Roderick SL, Matthews BW
Biochemistry 32 3907-12 (1993)
PMID: 8471602

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142397 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 264 amino acids
Theoretical weight: 29.37 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0AE18 (Residues: 1-264; Coverage: 100%)
Gene names: JW0163, b0168, map
Sequence domains: Metallopeptidase family M24
Structure domains: Creatinase/methionine aminopeptidase superfamily

Ligands and Environments

1 bound ligand:
Ligand CO 2 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 39Å b: 61.7Å c: 54.5Å
α: 90° β: 107.3° γ: 90°
R-values:
R R work R free
0.182 not available not available
Expression system: Not provided

Quick links

Citations

25 review citations

N-terminal processing: the methionine aminopeptidase and N alpha-acetyl transferase families.
Bradshaw et al. (1998)
24 more

7 mentions without citation

Advances in Bacterial Methionine Aminopeptidase Inhibition.
Helgren et al. (2016)
6 more