Crystallization and preliminary X-ray diffraction analysis of a novel sphingomyelinase D from Loxosceles gaucho venom

Acta Crystallogr F Struct Biol Commun. 2014 Oct;70(Pt 10):1418-20. doi: 10.1107/S2053230X14019207. Epub 2014 Sep 25.

Abstract

Brown spider envenomation results in dermonecrosis, intravascular coagulation, haemolysis and renal failure, mainly owing to the action of sphingomyelinases D (SMases D), which catalyze the hydrolysis of sphingomyelin to produce ceramide 1-phosphate and choline or the hydrolysis of lysophosphatidylcholine to produce lysophosphatidic acid. Here, the heterologous expression, purification, crystallization and preliminary X-ray diffraction analysis of LgRec1, a novel SMase D from Loxosceles gaucho venom, are reported. The crystals belonged to space group P21212, with unit-cell parameters a = 52.98, b = 62.27, c = 84.84 Å and diffracted to a maximum resolution of 2.6 Å.

Keywords: Loxosceles gaucho; sphingomyelinase D.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Arthropod Proteins / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Phosphoric Diester Hydrolases / chemistry*
  • Spider Venoms / enzymology*

Substances

  • Arthropod Proteins
  • Spider Venoms
  • Phosphoric Diester Hydrolases
  • sphingomyelin phosphodiesterase D