› 6mrq

X-ray diffraction
1.29Å resolution

Structure of ToPI1 inhibitor from Tityus obscurus scorpion venom in complex with trypsin

Released:
DOI: 10.2210/pdb6mrq/pdb
PDB entry 6mrq coloured by chain, front view.
PDB entry 6mrq coloured by chain, side view.
PDB entry 6mrq coloured by chain, top view.
Source organisms:
Primary publication:
Head-to-Tail Cyclization after Interaction with Trypsin: A Scorpion Venom Peptide that Resembles Plant Cyclotides.
Mourão CBF, Brand GD, Fernandes JPC, Prates MV, Bloch C, Barbosa JARG, Freitas SM, Restano-Cassulini R, Possani LD, Schwartz EF
J Med Chem 63 9500-9511 (2020)
PMID: 32787139

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Arg-|-, Lys-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-279405 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease 1 Chain: A
Molecule details ›
Chain: A
Length: 237 amino acids
Theoretical weight: 24.93 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00760 (Residues: 24-246; Coverage: 97%)
Gene names: PRSS1, TRP1, TRY1, TRYP1
Sequence domains: Trypsin
inhibitor from Tityus obscurus scorpion venom (TopI1) Chain: I
Molecule details ›
Chain: I
Length: 32 amino acids
Theoretical weight: 3.74 KDa
Source organism: Tityus
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P212121
Unit cell:
a: 46.817Å b: 59.02Å c: 79.085Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.165 0.18
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

5 review citations

Therapeutic peptides: current applications and future directions.
Wang et al. (2022)
4 more

1 mention without citation

Amazonian scorpions and scorpionism: integrating toxinological, clinical, and phylogenetic data to combat a human health crisis in the world's most diverse rainfores.
Borges et al. (2021)