Structural Resolution of the Complex between a Fungal Polygalacturonase and a Plant Polygalacturonase-Inhibiting Protein by Small-Angle X-Ray Scattering  | Zendy

Manuel Benedetti | Zendy; Claudia Leggio | Zendy; Luca Federici | Zendy; Giulia De Lorenzo | Zendy; Nicolae Viorel Pavel | Zendy; Felice Cervone | Zendy

Open Access

Structural Resolution of the Complex between a Fungal Polygalacturonase and a Plant Polygalacturonase-Inhibiting Protein by Small-Angle X-Ray Scattering

Author(s) -

Manuel Benedetti,

Claudia Leggio,

Luca Federici,

Giulia De Lorenzo,

Nicolae Viorel Pavel,

Felice Cervone

Publication year - 2011

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.111.181057

Subject(s) - pectinase , phaseolus , mutagenesis , enzyme , resolution (logic) , biochemistry , site directed mutagenesis , biology , chemistry , botany , mutation , gene , artificial intelligence , computer science , mutant

We report here the low-resolution structure of the complex formed by the endo-polygalacturonase from Fusarium phyllophilum and one of the polygalacturonase-inhibiting protein from Phaseolus vulgaris after chemical cross-linking as determined by small-angle x-ray scattering analysis. The inhibitor engages its concave surface of the leucine-rich repeat domain with the enzyme. Both sides of the enzyme active site cleft interact with the inhibitor, accounting for the competitive mechanism of inhibition observed. The structure is in agreement with previous site-directed mutagenesis data and has been further validated with structure-guided mutations and subsequent assay of the inhibitory activity. The structure of the complex may help the design of inhibitors with improved or new recognition capabilities to be used for crop protection.

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