1te1

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spinqualitylabelsall models 1te1, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of family 11 xylanase in complex with inhibitor (XIP-I)

Overview

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 A 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. Inhibition of the GH11 xylanase is mediated by the insertion of an, XIP-I Pi-shaped loop (Lalpha(4)beta(5)) into the enzyme active site, whereas residues in the helix alpha7 of XIP-I, pointing into the four, central active site subsites, are mainly responsible for the reversible, inactivation of GH10 xylanases. The XIP-I strategy for inhibition of, xylanases involves substrate-mimetic contacts and interactions occluding, the active site. The structural determinants of XIP-I specificity, demonstrate that the inhibitor is able to interact with GH10 and GH11, xylanases of both fungal and bacterial origin. The biological role of the, xylanase inhibitors is discussed in light of the present structural data.

About this Structure

1TE1 is a Protein complex structure of sequences from Penicillium funiculosum and Triticum aestivum with NAG and EDO as ligands. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Full crystallographic information is available from OCA.

Reference

The dual nature of the wheat xylanase protein inhibitor XIP-I: structural basis for the inhibition of family 10 and family 11 xylanases., Payan F, Leone P, Porciero S, Furniss C, Tahir T, Williamson G, Durand A, Manzanares P, Gilbert HJ, Juge N, Roussel A, J Biol Chem. 2004 Aug 20;279(34):36029-37. Epub 2004 Jun 4. PMID:15181003

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