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首页> 外文期刊>Glycobiology >LysM domains of Medicago truncatula NFP protein involved in Nod factor perception. Glycosylation state, molecular modeling and docking of chitooligosaccharides and Nod factors
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LysM domains of Medicago truncatula NFP protein involved in Nod factor perception. Glycosylation state, molecular modeling and docking of chitooligosaccharides and Nod factors

机译：run藜NFP蛋白的LysM结构域参与Nod因子感知。壳寡糖和Nod因子的糖基化状态，分子建模和对接

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摘要

The establishment of the symbiosis between legume plants and rhizobial bacteria depends on the production of rhizobial lipo-chitooligosaccharidic signals (the Nod factors) that are specifically recognized by roots of the host plant. In Medicago truncatula, specific recognition of Sinorhizobium meliloti and its Nod factors requires the NFP (Nod factor perception) gene, which encodes a putative serine/threonine receptor-like kinase (RLK). The extracellular region of this protein contains three tandem lysin motifs (LysMs), a short peptide domain that is implicated in peptidoglycan or chitin binding in various bacterial or eukaryotic proteins, respectively. We report here the homology modeling of the three LysM domains of M. truncatula NFP based on the structure of a LysM domain of the Escherichia coli membrane-bound lytic murein transglycosidase D (MltD). Expression of NFP in a homologous system (M. truncatula roots) revealed that the protein is highly N‐glycosylated, probably with both high-mannose and complex glycans. Surface analysis and docking calculations performed on the models of the three domains were used to predict the most favored binding modes for chitooligosaccharides and Nod factors. A convergent model can be proposed where the sulfated, O-acetylated lipo-chitooligosaccharidic Nod factor of S. meliloti binds in similar orientation to the three LysM domains of M. truncatula NFP. N-glycosylation is not expected to interfere with Nod factor binding in this orientation.
机译：豆科植物和根瘤菌之间的共生关系的建立取决于宿主植物根部特异性识别的根瘤菌脂-壳寡糖信号（Nod因子）的产生。在run藜苜蓿中，对中华根瘤菌及其Nod因子的特异性识别需要NFP（Nod因子感知）基因，该基因编码一种假定的丝氨酸/苏氨酸受体样激酶（RLK）。该蛋白的细胞外区域包含三个串联的溶素基序（LysMs），这是一个短肽域，分别与各种细菌或真核蛋白中的肽聚糖或几丁质结合有关。我们在这里报告了基于大肠杆菌膜结合的溶血性murein转糖苷酶D（MltD）的LysM域的结构的M. truncatula NFP的三个LysM域的同源性建模。 NFP在同源系统（M. truncatula根）中的表达表明该蛋白高度N-糖基化，可能同时含有高甘露糖和复杂聚糖。在这三个域的模型上进行的表面分析和对接计算可用于预测壳寡糖和Nod因子的最佳结合方式。可以提出一个收敛模型，其中苜蓿链球菌的硫酸化的，O-乙酰化的脂-壳寡糖的Nod因子以相似的方向结合到截枝分枝杆菌NFP的三个LysM结构域上。 N-糖基化预期不会在此方向上干扰Nod因子结合。

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  • 来源
    《Glycobiology》 |2006年第9期|801-809|共9页
  • 作者

    Lonneke Mulder; Benoit Lefebvre; Julie Cullimore; and Anne Imberty;

  • 作者单位

    Laboratoire des Interactions Plantes-Microorganismes INRA-CNRS BP 52627 31326 Castanet-Tolosan Cedex France;

    and;

    Centre de Recherches sur les Macromolécules Végétales CNRS (affiliated with Université Joseph Fourier) 601 rue de la Chimie BP 53 38041 Grenoble Cedex 9 France;

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