• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Solution structure, backbone dynamics and chitin binding of the anti-fungal protein from Streptomyces tendae TU901.
【24h】

Solution structure, backbone dynamics and chitin binding of the anti-fungal protein from Streptomyces tendae TU901.

机译：链霉菌TU901的抗真菌蛋白的溶液结构，骨架动力学和几丁质结合。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

AFP1 is a recently discovered anti-fungal, chitin-binding protein from Streptomyces tendae Tu901. Mature AFP1 comprises 86 residues and exhibits limited sequence similarity to the cellulose-binding domains of bacterial cellulases and xylanases. No similarity to the Cys and Gly-rich domains of plant chitin-binding proteins (e.g. agglutinins, lectins, hevein) is observed. AFP1 is the first chitin-binding protein from a bacterium for which anti-fungal activity was shown. Here, we report the three-dimensional solution structure of AFP1, determined by nuclear magnetic resonance spectroscopy. The protein contains two antiparallel beta-sheets (five and four beta-strands each), that pack against each other in a parallel beta-sandwich. This type of architecture is conserved in the functionally related family II of cellulose-binding domains, albeit with different connectivity. A similar fold is also observed in other unrelated proteins (spore coat protein from Myxococcus xanthus, beta-B2 and gamma-B crystallins from Bos taurus, canavalin from Jack bean). AFP1 is therefore classified as a new member of the betagamma-crystallin superfamily. The dynamics of the protein was characterized by NMR using amide 15N relaxation and solvent exchange data. We demonstrate that the protein exhibits an axially symmetric (oblate-like) rotational diffusion tensor whose principal axis coincides to within 15 degrees with that of the inertial tensor. After completion of the present structure of AFP1, an identical fold was reported for a Streptomyces killer toxin-like protein. Based on sequence comparisons and clustering of conserved residues on the protein surface for different cellulose and chitin-binding proteins, we postulate a putative sugar-binding site for AFP1. The inability of the protein to bind short chitin fragments suggests that certain particular architectural features of the solid chitin surface are crucial for the interaction. Copyright 2001 Academic Press.
机译：AFP1是最近发现的来自链霉菌Tu901的抗真菌几丁质结合蛋白。成熟的AFP1包含86个残基，并且与细菌纤维素酶和木聚糖酶的纤维素结合结构域具有有限的序列相似性。没有观察到与植物几丁质结合蛋白（例如凝集素，凝集素，肝素）的富含Cys和Gly的结构域的相似性。 AFP1是来自细菌的第一个几丁质结合蛋白，其具有抗真菌活性。在这里，我们报告AFP1的三维解决方案结构，由核磁共振波谱确定。该蛋白质包含两个反平行的β-折叠（每个有五个和四个β-链），它们以平行的β-三明治相互堆积。尽管具有不同的连接性，但这种类型的结构在功能相关的纤维素结合域家族II中是保守的。在其他不相关的蛋白质中也观察到了类似的折叠（来自黄色葡萄球菌的孢子外壳蛋白，来自金牛座的β-B2和γ-B结晶蛋白，来自杰克豆的canavalin）。因此，AFP1被分类为betagamma-crystallin超家族的新成员。使用酰胺15N弛豫和溶剂交换数据通过NMR表征蛋白质的动力学。我们证明该蛋白质表现出一个轴对称（扁圆状）旋转扩散张量，其主轴与惯性张量的主轴重合在15度以内。在完成本发明的AFP1结构后，报道了链霉菌杀手毒素样蛋白的相同折叠。基于序列比较和不同的纤维素和几丁质结合蛋白的蛋白质表面上保守残基的聚类，我们推测AFP1的假定糖结合位点。该蛋白质不能结合几丁质短片段，这表明固体几丁质表面的某些特定结构特征对于相互作用至关重要。版权所有2001学术出版社。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号