› 3t8w

X-ray diffraction
2Å resolution

A bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases

Released:
DOI: 10.2210/pdb3t8w/pdb
PDB entry 3t8w coloured by chain, front view.
PDB entry 3t8w coloured by chain, side view.
PDB entry 3t8w coloured by chain, top view.
Source organism: Plasmodium falciparum 3D7
Primary publication:
Bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases.
Harbut MB, Velmourougane G, Dalal S, Reiss G, Whisstock JC, Onder O, Brisson D, McGowan S, Klemba M, Greenbaum DC
Proc Natl Acad Sci U S A 108 E526-34 (2011)
PMID: 21844374

Function and Biology Details

Reaction 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.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184810 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leucine aminopeptidase Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 528 amino acids
Theoretical weight: 58.71 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8IL11 (Residues: 84-605; Coverage: 86%)
Gene names: LAP, PF3D7_1446200
Sequence domains: Cytosol aminopeptidase family, catalytic domain
Structure domains:

Ligands and Environments

6 bound ligands:
Ligand CO3 12 x CO3
Ligand ZN 24 x ZN
Ligand DGZ 12 x DGZ
Ligand SO4 29 x SO4
Ligand 1PE 33 x 1PE
Ligand 2PE 2 x 2PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P212121
Unit cell:
a: 173.748Å b: 177.057Å c: 231.221Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.2
Expression system: Escherichia coli

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Citations

14 review citations

New approaches for dissecting protease functions to improve probe development and drug discovery.
Deu et al. (2012)
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4 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
3 more