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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The binding specificity and affinity determinants of family 1 and family 3 cellulose binding modules.
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The binding specificity and affinity determinants of family 1 and family 3 cellulose binding modules.

机译：1族和3族纤维素结合模块的结合特异性和亲和力决定因素。

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摘要

Cellulose binding modules (CBMs) potentiate the action of cellulolytic enzymes on insoluble substrates. Numerous studies have established that three aromatic residues on a CBM surface are needed for binding onto cellulose crystals and that tryptophans contribute to higher binding affinity than tyrosines. However, studies addressing the nature of CBM-cellulose interactions have so far failed to establish the binding site on cellulose crystals targeted by CBMs. In this study, the binding sites of CBMs on Valonia cellulose crystals have been visualized by transmission electron microscopy. Fusion of the CBMs with a modified staphylococcal protein A (ZZ-domain) allowed direct immuno-gold labeling at close proximity of the actual CBM binding site. The transmission electron microscopy images provide unequivocal evidence that the fungal family 1 CBMs as well as the family 3 CBM from Clostridium thermocellum CipA have defined binding sites on two opposite corners of Valonia cellulose crystals. In most samples these corners are worn to display significant area of the hydrophobic (110) plane, which thus constitutes the binding site for these CBMs.
机译：纤维素结合模块（CBM）增强了纤维素酶在不溶性底物上的作用。大量研究表明，CBM表面需要三个芳族残基才能与纤维素晶体结合，色氨酸比酪氨酸具有更高的结合亲和力。然而，迄今为止，针对CBM-纤维素相互作用的性质的研究未能在CBM靶向的纤维素晶体上建立结合位点。在这项研究中，通过透射电子显微镜可以看到CBM在Valonia纤维素晶体上的结合位点。 CBM与修饰的葡萄球菌蛋白A（ZZ-结构域）的融合允许在实际CBM结合位点的紧邻处直接免疫金标记。透射电子显微镜图像提供了明确的证据，即来自热纤梭菌CipA的真菌家族1 CBM和家族3 CBM在Valonia纤维素晶体的两个相对角上定义了结合位点。在大多数样品中，这些角部被磨损以显示疏水性（110）平面的显着区域，因此构成了这些CBM的结合位点。

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