1T6E

Crystal Structure of the Triticum aestivum xylanase inhibitor I

Summary for 1T6E

• Entry DOI: 10.2210/pdb1t6e/pdb
• Descriptor: xylanase inhibitor, GLYCEROL (3 entities in total)
• Functional Keywords: two beta-barrel domain structure, hydrolase inhibitor
• Biological source: Triticum aestivum (bread wheat)
• Total number of polymer chains: 1
• Total formula weight: 38954.62

Authors

Sansen, S.,De Ranter, C.J.,Gebruers, K.,Brijs, K.,Courtin, C.M.,Delcour, J.A.,Rabijns, A. (deposition date: 2004-05-06, release date: 2004-09-28, Last modification date: 2024-11-20)

Primary citation

Sansen, S.,De Ranter, C.J.,Gebruers, K.,Brijs, K.,Courtin, C.M.,Delcour, J.A.,Rabijns, A.
Structural basis for inhibition of Aspergillus niger xylanase by triticum aestivum xylanase inhibitor-I
J.Biol.Chem., 279:36022-36028, 2004

PubMed Abstract: 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.

PubMed: 15166216
DOI: 10.1074/jbc.M404212200

Experimental method

X-RAY DIFFRACTION (1.7 Å)