Producción CyT

Crystallization and preliminary X-ray study of the common edible mushroom (Agaricus bisporus) lectin.

Artículo

Autoría:

CARRIZO ME, ; IRAZOQUI, FERNANDO JOSE ; LARDONE RD, ; NORES GA, ; CURTINO JA, ; CAPALDI S, ; PERDUCA M, ; MONACO HL,

Fecha:

2004

Revista:

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, vol. 60 (pp. 718-720)

Resumen *

Crystallization and preliminary X-ray study of the common edible mushroom ( Agaricus bisporus) lectin Maria E. Carrizo, Fernando J. Irazoqui, Ricardo D. Lardone, Gustavo A. Nores, Juan A. Curtino, Stefano Capaldi, Massimiliano Perduca and Hugo L. Monaco Acta Crystallographica Section D Biological Crystallography (2004). D60, 718–720 ISSN 0907-4449 Editors: E. N. Baker and Z. Dauter The lectin from the common edible mushroom Agaricus bisporus (ABL) belongs to the group of proteins that have the property of binding the Thomsen±Friedenreich antigen (T-antigen) selectively and with high afÆnity, but does not show any sequence similarity to the other proteins that share this property. The ABL sequence is instead similar to those of members of the saline-soluble fungal lectins, a protein family with pesticidal properties. The presence of different isoforms has been reported. It has been found that in order to be able to grow diffraction-quality crystals of the lectin, it is essential to separate the isoforms, which was performed by preparative isoelectric focusing. Using standard procedures, it was possible to crystallize the most basic of the forms by either vapour diffusion or equilibrium dialysis, but attempts to grow crystals of the other more acidic forms were unsuccessful. The ABL crystals belong to the orthorhombic space group C2221, with unit-cell parameters a = 93.06, b = 98.16, c = 76.38 A , and diffract to a resolution of 2.2 A on a conventional source at room temperature. It is expected that the solution of this structure will yield further valuable information on the differences in the T-antigen-binding folds and will perhaps help to clarify the details of the ligand binding to the protein. Información suministrada por el agente en SIGEVA