Crystallization and preliminary X-ray diffraction analysis of a novel Arg49 phospholipase A2 homologue from Zhaoermia mangshanensis venom

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jul 1;63(Pt 7):605-7. doi: 10.1107/S1744309107026073. Epub 2007 Jun 22.

Abstract

Zhaoermiatoxin, an Arg49 phospholipase A2 homologue from Zhaoermia mangshanensis (formerly Trimeresurus mangshanensis, Ermia mangshanensis) venom is a novel member of the PLA2-homologue family that possesses an arginine residue at position 49, probably arising from a secondary Lys49-->Arg substitution that does not alter the catalytic inactivity towards phospholipids. Like other Lys49 PLA2 homologues, zhaoermiatoxin induces oedema and strong myonecrosis without detectable PLA2 catalytic activity. A single crystal with maximum dimensions of 0.2 x 0.2 x 0.5 mm was used for X-ray diffraction data collection to a resolution of 2.05 A using synchrotron radiation and the diffraction pattern was indexed in the hexagonal space group P6(4), with unit-cell parameters a = 72.9, b = 72.9, c = 93.9 A.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution / genetics
  • Animals
  • Arginine / chemistry*
  • Crotalid Venoms / enzymology*
  • Crotalid Venoms / genetics
  • Crystallization
  • Male
  • Phospholipases A / chemistry*
  • Phospholipases A / genetics
  • Phospholipases A2
  • Structural Homology, Protein*
  • Trimeresurus* / genetics
  • X-Ray Diffraction

Substances

  • Crotalid Venoms
  • Trimeresurus venoms
  • Arginine
  • Phospholipases A
  • Phospholipases A2