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

Metadata-grounded summary

Citation 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 P4(3)2(1)2 or P4(1)2(1)2, with unit-cell parameters a = b = 96.92, c = 61.42 A. The crystal contains two molecules per asymmetric unit and diffracts to 1.4 A resolution when exposed to synchrotron radiation.