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Crystallization and preliminary X-ray crystallographic studies on the fungal immunomodulatory protein Fve from the golden needle mushroom (Flammulina velutipes)

  • See Voon Seow
  • , I. Chun Kuo
  • , Palasingam Paaventhan
  • , Prasanna R. Kolatkar
  • , Kaw Yan Chua*
  • *Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

The fungal immunomodulatory protein from the edible golden needle mushroom (Flammulina velutipes), designated Fve, is a single polypeptide consisting of 114 amino-acid residues. It is believed to trigger the mitogenic proliferation of T lymphocytes and Th1 cytokine production. Here, it is demonstrated that Fve forms a homodimer in nature. In order to understand the relationship between its structure and function, Fve was crystallized using the hanging-drop method; the protein formed well diffracting crystals within 3-5 d in 2.5% PEG 400, 2.0 M ammonium sulfate and 0.1 M Tris base buffer pH 8.5. The space group of the Fve crystals is either P43212 or P412 12, with unit-cell parameters a =- b = 96.92, c = 61.42 Å. The crystal contains two molecules per asymmetric unit and diffracts to 1.4 Å resolution when exposed to synchrotron radiation.

Original languageEnglish
Pages (from-to)1487-1489
Number of pages3
JournalActa Crystallographica Section D: Structural Biology
Volume59
Issue number8
DOIs
Publication statusPublished - 1 Aug 2003
Externally publishedYes

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