利用小角 X 射线散射解析真菌多聚半乳糖醛酸酶与植物多聚半乳糖醛酸酶抑制蛋白复合物的结构
Structural resolution of the complex between a fungal polygalacturonase and a plant polygalacturonase-inhibiting protein by small-angle X-ray scattering.
机构信息
Dipartimento di Biologia e Biotecnologie C. Darwin, Istituto Pasteur-Fondazione Cenci Bolognetti, Sapienza Università di Roma, 00185 Rome, Italy.
出版信息
Plant Physiol. 2011 Oct;157(2):599-607. doi: 10.1104/pp.111.181057. Epub 2011 Aug 22.
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.
摘要
我们在此报告了经过化学交联后，由尖孢镰刀菌内切多聚半乳糖醛酸酶和菜豆多聚半乳糖醛酸酶抑制蛋白之一形成的复合物的低分辨率结构，该结构通过小角 X 射线散射分析确定。抑制剂通过富含亮氨酸重复结构域的凹面与酶结合。酶活性位点裂缝的两侧都与抑制剂相互作用，这解释了观察到的抑制竞争机制。该结构与以前的定点突变数据一致，并通过结构指导突变和随后的抑制活性测定得到了进一步验证。该复合物的结构可能有助于设计具有改进或新识别能力的抑制剂，用于作物保护。
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