Properties of TAXI-type endoxylanase inhibitors

Gebruers, Kurt; Brijs, Kristof; Courtin, Christophe M.; Fierens, Katleen; Goesaert, Hans; Rabijns, A.; Raedschelders, Gert; Robben, Johan; Sansen, Stefaan; Sørensen, Jens F.; Campenhout, Steven Van; Delcour, Jan A.

doi:10.1016/j.bbapap.2003.08.013

Cited by 110 publications

(80 citation statements)

References 63 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Structure of A. nidulans Xylanase (XLNC)-The A. nidulans xylanase displays the typical (␤/␣) 8 TIM-barrel fold of GH10 xylanases (Fig. 1A).…”

Section: Overall Structuresmentioning

confidence: 99%

“…GH11 enzymes are ␤-jelly roll proteins in which the substrate-binding groove is formed by the concave face of one of the ␤-sheets (see Ref. 5, for example), whereas GH10 xylanases are (␤/␣) 8 barrels with the two catalytic glutamate residues located at the C termini of strands ␤4 and ␤7 (see Ref. 6, for example).…”

Section: The Xylanase Inhibitor Protein I (Xip-i) From Wheatmentioning

confidence: 99%

“…The crystal structure of XIP-I was recently determined to 1.8 Å resolution (12). The inhibitor has a (␤/␣) 8 barrel fold and displays structural features typical of the glycoside hydrolase family 18. Although the catalytic glutamate of GH18 chitinases is conserved in XIP-I, structural differences in the region homologous to the active site of chitinases probably account for the lack of activity of XIP-I toward chitin (12).…”

Section: The Xylanase Inhibitor Protein I (Xip-i) From Wheatmentioning

confidence: 99%

“…Recently, two families of plant proteins, designated as XIP and TAXI, have been shown to inhibit xylanases (7,8). XIP-I from wheat (Triticum aestivum) is the prototype of a novel class of "chitinase-like" cereal inhibitors that apparently inhibits reversibly fungal but not bacterial GH10 and GH11 xylanases (9 -11).…”

Section: The Xylanase Inhibitor Protein I (Xip-i) From Wheatmentioning

confidence: 99%

See 3 more Smart Citations

The Dual Nature of the Wheat Xylanase Protein Inhibitor XIP-I

Payan

Leone

Porciero

et al. 2004

Journal of Biological Chemistry

115

View full text Add to dashboard Cite

The xylanase inhibitor protein I (XIP-I) from wheatTriticum 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 Å 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 ⌸-shaped loop (L␣ 4 ␤ 5 ) into the enzyme active site, whereas residues in the helix ␣7 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.

show abstract

“…Structure of A. nidulans Xylanase (XLNC)-The A. nidulans xylanase displays the typical (␤/␣) 8 TIM-barrel fold of GH10 xylanases (Fig. 1A).…”

Section: Overall Structuresmentioning

confidence: 99%

Section: The Xylanase Inhibitor Protein I (Xip-i) From Wheatmentioning

confidence: 99%

Section: The Xylanase Inhibitor Protein I (Xip-i) From Wheatmentioning

confidence: 99%

Section: The Xylanase Inhibitor Protein I (Xip-i) From Wheatmentioning

confidence: 99%

See 2 more Smart Citations

The Dual Nature of the Wheat Xylanase Protein Inhibitor XIP-I

Payan

Leone

Porciero

et al. 2004

Journal of Biological Chemistry

115

View full text Add to dashboard Cite

show abstract

“…Since neither type of inhibitor has the ability to inhibit wheat endogenous xylanases, 5) it has been speculated that they are involved in plant defense against fungal pathogens. 3,6) But there was no evidence of pathogenesis-related features of Xip and Taxi, 6) and individual family member genes with pathogen-responsive expression remained to be identified. Recently, we demonstrated the presence of multiple TAXI-type genes in wheat with the isolation of two new family members, Taxi-III and Taxi-IV.…”

mentioning

confidence: 99%