Purification, partial characterization and crystallization of acucetin, a protein containing both disintegrin-like and cysteine-rich domains released by auto-proteolysis of a P-III-type metalloproteinase AaH-IV from Agkistrodon acutus venom

Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2310-2. doi: 10.1107/s0907444903020626. Epub 2003 Nov 27.

Abstract

AaH-IV, a P-III-type metalloproteinase found in Agkistrodon acutus venom, readily cleaves itself to release a stable protein named acucetin at 310 K under neutral and weakly alkaline conditions. A partial amino-acid residue sequence of acucetin indicates that the protein has a high homology to snake-venom proteins containing both disintegrin-like and cysteine-rich domains. Acucetin has been crystallized in space group R32, with hexagonal unit-cell parameters a = b = 155.98, c = 76.07 A. The V(M) value of about 2.97 A(3) Da(-1) suggests the presence of only one molecule in the asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agkistrodon
  • Amino Acid Sequence
  • Animals
  • Crotalid Venoms / chemistry*
  • Crotalid Venoms / enzymology
  • Crystallization
  • Crystallography, X-Ray
  • Cysteine / chemistry
  • Cysteine / genetics
  • Disintegrins / chemistry
  • Disintegrins / genetics
  • Metalloendopeptidases / chemistry*
  • Metalloendopeptidases / genetics
  • Metalloendopeptidases / metabolism
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Sequence Analysis, Protein

Substances

  • Crotalid Venoms
  • Disintegrins
  • Metalloendopeptidases
  • Cysteine