Crystallization and preliminary X-ray diffraction analysis of myotoxin I, a Lys49-phospholipase A2 from Bothrops moojeni

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Oct 1;61(Pt 10):882-4. doi: 10.1107/S174430910502717X. Epub 2005 Sep 13.

Abstract

A new myotoxic Lys49-phospholipase A2 isolated from Bothrops moojeni snake venom has been crystallized. The crystals diffracted to 2.18 A resolution using a synchrotron-radiation source and belong to space group C2. The unit-cell parameters are a = 56.8, b = 125.0, c = 64.7 A, beta = 105.5 degrees. Preliminary analysis indicates the presence of four molecules in the asymmetric unit. This may suggest a new quaternary structure for this Lys49-phospholipase A2 in contrast to the dimeric and monomeric structures solved so far for this class of proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Crystallization
  • Crystallography, X-Ray
  • Diffusion
  • Dimerization
  • Electrophoresis, Polyacrylamide Gel
  • Group II Phospholipases A2
  • Isoelectric Focusing
  • Lysine / chemistry*
  • Phospholipases A / chemistry*
  • Protein Conformation
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Reptilian Proteins
  • Snake Venoms / metabolism*
  • Snakes
  • Synchrotrons
  • X-Ray Diffraction

Substances

  • Reptilian Proteins
  • Snake Venoms
  • Phospholipases A
  • Group II Phospholipases A2
  • myotoxin I
  • Lysine