› 3h8g

X-ray diffraction
1.5Å resolution

Bestatin complex structure of leucine aminopeptidase from Pseudomonas putida

Released:
DOI: 10.2210/pdb3h8g/pdb
PDB entry 3h8g coloured by chain, front view.
PDB entry 3h8g coloured by chain, side view.
PDB entry 3h8g coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Crystal structure of the leucine aminopeptidase from Pseudomonas putida reveals the molecular basis for its enantioselectivity and broad substrate specificity.
Kale A, Pijning T, Sonke T, Dijkstra BW, Thunnissen AM
J Mol Biol 398 703-14 (2010)
PMID: 20359484

Function and Biology Details

Reactions catalysed: 
Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131474 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytosol aminopeptidase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 497 amino acids
Theoretical weight: 52.53 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
  • Canonical: O86436 (Residues: 1-497; Coverage: 100%)
Gene name: pepA
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand ZN 6 x ZN
Ligand MN 6 x MN
Ligand K 6 x K
Ligand BCT 6 x BCT
Ligand BES 6 x BES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P1
Unit cell:
a: 95.976Å b: 95.989Å c: 95.998Å
α: 100.82° β: 107.78° γ: 93.23°
R-values:
R R work R free
0.151 0.149 0.173
Expression system: Escherichia coli

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Citations

10 citation in other articles

A manganese-rich environment supports superoxide dismutase activity in a Lyme disease pathogen, Borrelia burgdorferi.
Aguirre et al. (2013)
9 more

6 mentions without citation

Marine Invertebrates: A Promissory Still Unexplored Source of Inhibitors of Biomedically Relevant Metallo Aminopeptidases Belonging to the M1 and M17 Families.
Pascual Alonso et al. (2023)
5 more