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      Structural resolution of the complex between a fungal polygalacturonase and a plant polygalacturonase-inhibiting protein by small-angle X-ray scattering.

      Plant physiology

      Catalytic Domain, Enzyme Inhibitors, chemistry, metabolism, Fungal Proteins, Fusarium, enzymology, Host-Pathogen Interactions, Mutagenesis, Site-Directed, Phaseolus, Plant Proteins, genetics, Polygalacturonase, Protein Conformation, Scattering, Small Angle, X-Ray Diffraction

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          Abstract

          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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          Author and article information

          Journal
          21859985
          3192570
          10.1104/pp.111.181057

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