1t6g
From Proteopedia
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Crystal structure of the Triticum aestivum xylanase inhibitor-I in complex with aspergillus niger xylanase-I
Overview
Plants developed a diverse battery of defense mechanisms in response to, continual challenges by a broad spectrum of pathogenic microorganisms., Their defense arsenal includes inhibitors of cell wall-degrading enzymes, which hinder a possible invasion and colonization by antagonists. The, structure of Triticum aestivum xylanase inhibitor-I (TAXI-I), a first, member of potent TAXI-type inhibitors of fungal and bacterial family 11, xylanases, has been determined to 1.7-A resolution. Surprisingly, TAXI-I, displays structural homology with the pepsin-like family of aspartic, proteases but is proteolytically nonfunctional, because one or more, residues of the essential catalytical triad are absent. The structure of, the TAXI-I.Aspergillus niger xylanase I complex, at a resolution of 1.8 A, illustrates the ability of tight binding and inhibition with subnanomolar, affinity and indicates the importance of the C-terminal end for the, differences in xylanase specificity among different TAXI-type inhibitors.
About this Structure
1T6G is a Protein complex structure of sequences from Aspergillus niger and Triticum aestivum with GOL as ligand. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Full crystallographic information is available from OCA.
Reference
Structural basis for inhibition of Aspergillus niger xylanase by triticum aestivum xylanase inhibitor-I., Sansen S, De Ranter CJ, Gebruers K, Brijs K, Courtin CM, Delcour JA, Rabijns A, J Biol Chem. 2004 Aug 20;279(34):36022-8. Epub 2004 May 27. PMID:15166216
Page seeded by OCA on Wed Nov 21 03:01:12 2007
