Crystallization and preliminary X-ray studies of oligandrin, a sterol-carrier elicitor from Pythium oligandrum

Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1498-500. doi: 10.1107/s0907444900011744.

Abstract

Oligandrin is a 10 kDa acidic protein produced by the fungus micromycete Pythium oligandrum and is a member of the alpha-elicitin group, with sterol- and lipid-carrier properties. Oligandrin has been crystallized at 290 K using PEG 4000 as a precipitant. A cholesterol complex was obtained under the same conditions. The space group of the crystals at low temperature (100 K) is C222, with unit-cell parameters a = 94.0, b = 171.1, c = 55.3 A. Four molecules are present in the asymmetric unit. Data from the free and cholesterol-complexed forms were recorded at synchrotron sources to resolutions of 2.4 (uncomplexed) and 1.9 A (complexed), respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism
  • Cholesterol / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Electrophoresis, Polyacrylamide Gel
  • Fungal Proteins / chemistry*
  • Fungal Proteins / isolation & purification
  • Intercellular Signaling Peptides and Proteins
  • Protein Conformation
  • Pythium / chemistry*
  • Sterols / metabolism*

Substances

  • Carrier Proteins
  • Fungal Proteins
  • Intercellular Signaling Peptides and Proteins
  • Oligandrin protein, Pythium oligandrum
  • Sterols
  • Cholesterol