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首页> 外文期刊>The FEBS journal >O-glycosylation effects on family 1 carbohydrate-binding module solution structures
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O-glycosylation effects on family 1 carbohydrate-binding module solution structures

机译：O-糖基化对家族1碳水化合物结合模块溶液结构的影响

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摘要

Family 1 carbohydrate-binding modules (CBMs) are ubiquitous components of multimodular fungal enzymes that degrade plant cell wall polysaccharides and bind specifically to cellulose. Native glycosylation of family 1 CBMs has been shown to substantially impact multiple physical properties, including thermal and proteolytic stability and cellulose binding affinity. To gain molecular insights into the changes in CBM properties upon glycosylation, solution structures of two glycoforms of a Trichoderma reesei family 1 CBM were studied by NMR spectroscopy: a glycosylated family 1 CBM with a mannose group attached to both Thr1 and Ser3 and a second family 1 CBM with single mannose groups attached to Thr1, Ser3 and Ser14. The structures clearly reveal that monosaccharides at both Ser3 and Ser14 on family 1 CBMs present additional cellulose binding platforms, similar to well-characterized aromatic residues at the binding interface, which align to the cellulose surface. These results are in agreement with previous experimental work demonstrating that glycans at Ser3 and Ser14 impart significant improvements in binding affinity. Additionally, detailed analysis of the NMR structures and molecular simulations indicates that the protein backbone of the CBM is not significantly altered by attachment of monosaccharides, and that the mannose attached to Ser14 may be more flexible than the mannose at Ser3. Overall, the present study reveals how family 1 CBM structures are affected by covalent attachment of monosaccharides, which are likely important post-translational modifications of these common subdomains of fungal plant cell wall degrading enzymes.
机译：家族1的碳水化合物结合模块（CBM）是降解植物细胞壁多糖并与纤维素特异性结合的多模块真菌酶的普遍成分。已经显示，家族1 CBM的天然糖基化实质上影响多种物理性质，包括热和蛋白水解稳定性和纤维素结合亲和力。为了获得分子对糖基化后煤层气特性变化的见解，通过核磁共振波谱学研究了里氏木霉1族煤层气的两种糖型的溶液结构：糖基化的1族煤层气，其甘露糖基团与Thr1和Ser3同时连接1个带有单甘露糖基团的CBM，分别连接到Thr1，Ser3和Ser14。该结构清楚地表明，家族1 CBM的Ser3和Ser14上的单糖均具有其他纤维素结合平台，类似于结合界面上特征明确的芳香族残基，与纤维素表面对齐。这些结果与先前的实验工作一致，表明Ser3和Ser14的聚糖可显着改善结合亲和力。此外，对NMR结构和分子模拟的详细分析表明，CBM的蛋白主链不会因单糖的附着而显着改变，并且与Ser14相连的甘露糖可能比在Ser3上的甘露糖更具柔性。总的来说，本研究揭示了单糖的共价连接如何影响家族1 CBM结构，这可能是真菌植物细胞壁降解酶的这些常见亚域的重要翻译后修饰。

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