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首页> 外文期刊>Journal of Molecular Biology >A New Lectin Family with Structure Similarity to Actinoporins Revealed by the Crystal Structure of Xerocomus chrysenteron Lectin XCL.
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A New Lectin Family with Structure Similarity to Actinoporins Revealed by the Crystal Structure of Xerocomus chrysenteron Lectin XCL.

机译：Xerocomus chrysenteron Lectin XCL的晶体结构揭示了一个与肌动孔蛋白结构相似的新凝集素家族。

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摘要

A newly defined family of fungal lectins displays no significant sequence similarity to any protein in the databases. These proteins, made of about 140 amino acid residues, have sequence identities ranging from 38% to 65% and share binding specificity to N-acetyl galactosamine. One member of this family, the lectin XCL from Xerocomus chrysenteron, induces drastic changes in the actin cytoskeleton after sugar binding at the cell surface and internalization, and has potent insecticidal activity. The crystal structure of XCL to 1.4A resolution reveals the architecture of this new lectin family. The fold of the protein is not related to any of the several lectin folds documented so far. Unexpectedly, the structure similarity is significant with actinoporins, a family of pore-forming toxins. The specific structural features and sequence signatures in each protein family suggest a potential sugar binding site in XCL and a possible evolutionary relationship between these proteins. Finally, the tetrameric assembly of XCL reveals a complex network of protomer-protomer interfaces and generates a large, hydrated cavity of 1000A(3), which may become accessible to larger solutes after a small conformational change of the protein.
机译：新定义的真菌凝集素家族与数据库中的任何蛋白质都没有显着的序列相似性。这些由约140个氨基酸残基组成的蛋白质具有38％至65％的序列同一性，并具有与N-乙酰半乳糖胺的结合特异性。该家族的一个成员，来自Xerocomus chrysenteron的凝集素XCL，在细胞表面结合糖并内化后，诱导肌动蛋白细胞骨架发生剧烈变化，并具有有效的杀虫活性。 XCL至1.4A分辨率的晶体结构揭示了该新凝集素家族的体系结构。蛋白质的折叠与迄今记录的几种凝集素折叠均不相关。出乎意料的是，与肌动孔蛋白（一种成孔毒素家族）的结构相似性很明显。每个蛋白质家族中的特定结构特征和序列特征表明XCL中可能存在糖结合位点，并且这些蛋白质之间可能存在进化关系。最后，XCL的四聚体组装揭示了一个复杂的protomer-protomer接口网络，并产生了一个大的水合空腔1000A（3），在蛋白质的构象发生微小变化后，较大的溶质可能会进入该空腔。

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