Cohesin‐dockerin recognition in cellulosome assembly: Experiment versus hypothesis
Cohesin‐dockerin recognition in cellulosome assembly: Experiment versus hypothesis
复制标题
纤维素体组装中的粘连蛋白-坞蛋白识别：实验与假设
DOI：
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发表时间：
2000
期刊：
影响因子：
--
通讯作者：
E. Bayer
中科院分区：
文献类型：
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作者：
A. Mechaly;S. Yaron;R. Lamed;H. Fierobe;A. Bélaich;J. Belaich;Y. Shoham;E. Bayer
粘着蛋白-锚定蛋白相互作用为将单个酶亚基掺入多纤维素酶体复合物提供了基础。在之前的文章中（Pagés et al.，Proteins 1997;29：517-527），我们预测了1070个残基的锚定蛋白结构域的4个氨基酸残基将作为与粘附蛋白结构域结合的识别代码。通过对可疑残基进行定点诱变来检查预测的有效性，从而改变了粘附素-锚定蛋白相互作用的种属特异性。结果支持的前提下，这四个残基确实发挥了生物识别的作用，而额外的残基也可能有助于相互作用的特异性。蛋白质2000;39：170-177.© 2000 Wiley利斯公司
The cohesin‐dockerin interaction provides the basis for incorporation of the individual enzymatic subunits into the cellulosome complex. In a previous article ( Pagés et al. , Proteins 1997;29:517–527) we predicted that four amino acid residues of the ∼70‐residue dockerin domain would serve as recognition codes for binding to the cohesin domain. The validity of the prediction was examined by site‐directed mutagenesis of the suspected residues, whereby the species‐specificity of the cohesin‐dockerin interaction was altered. The results support the premise that the four residues indeed play a role in biorecognition, while additional residues may also contribute to the specificity of the interaction. Proteins 2000;39:170–177. © 2000 Wiley‐Liss, Inc.
影响因子：
3.5
作者：
HO, SN;HUNT, HD;PEASE, LR
通讯作者：
PEASE, LR