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Payan, F ; Leone, P ; Porciero, S ; Furniss, C ; Tahir, T ; Williamson, G ; Durand, A ; Manzanares, P ; Gilbert, HJ ; Juge, N ; Roussel, A

The dual nature of the wheat xylanase protein inhibitor XIP-I - Structural basis for the inhibition of family 10 and family 11 xylanases

Journal of Biological Chemistry 279 (34) 36029-36037

par Administrateur - publié le

Abstract :

The xylanase inhibitor protein I (XIP-I) from wheat Triticum aestivum is the prototype of a novel class of cereal protein inhibitors that inhibit fungal xylanases belonging to glycoside hydrolase families 10 (GH10) and 11 (GH11). The crystal structures of XIP-I in complex with Aspergillus nidulans (GH10) and Penicillium funiculosum (GH11) xylanases have been solved at 1.7 and 2.5 Angstrom resolution, respectively. The inhibition strategy is novel because XIP-I possesses two independent enzyme-binding sites, allowing binding to two glycoside hydrolases that display a different fold.