PRIMARY SEQUENCE-ANALYSIS OF CLOSTRIDIUM-CELLULOVORANS CELLULOSE BINDING PROTEIN-A
PRIMARY SEQUENCE-ANALYSIS OF CLOSTRIDIUM-CELLULOVORANS CELLULOSE BINDING PROTEIN-A
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DOI：
10.1073/pnas.89.8.3483
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发表时间：
1992-04-15
影响因子：
11.1
通讯作者：
DOI, RH
中科院分区：
文献类型：
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作者：
SHOSEYOV, O;TAKAGI, M;DOI, RH
纤维素梭菌纤维素结合蛋白(CbpA)的CBPA基因是纤维素酶多亚基复合体的一部分，已被克隆和测序。当CBPA在大肠杆菌中表达时，观察到能够与结晶纤维素结合和与抗CbpA相互作用的蛋白质。CBPA基因全长5544个碱基对，编码1848个氨基酸，分子质量为189,036 Da。在开放阅读框架之前有一个革兰氏阳性核糖体结合位点。在其N端有一个28个氨基酸的信号肽序列。编码的蛋白质是高度疏水的，含有极高水平的苏氨酸和缬氨酸残基。有两种类型的假定的纤维素结合结构域，几乎等于-100个氨基酸，稍微亲水，以及8个保守的，高度疏水的β-折叠区域，几乎等于-140个氨基酸。后者可能是CbpA结构域，与纤维素酶复合体的不同酶亚基相互作用。
The cbpA gene for the Clostridium cellulovorans cellulose binding protein (CbpA), which is part of the multisubunit cellulase complex, has been cloned and sequenced. When cbpA was expressed in Escherichia coli, proteins capable of binding to crystalline cellulose and of interacting with anti-CbpA were observed. The cbpA gene consists of 5544 base pairs and encodes a protein containing 1848 amino acids with a molecular mass of 189,036 Da. The open reading frame is preceded by a Gram-positive-type ribosome binding site. A signal peptide sequence of 28 amino acids is present at its N terminus. The encoded protein is highly hydrophobic with extremely high levels of threonine and valine residues. There are two types of putative cellulose binding domains of almost-equal-to 100 amino acids that are slightly hydrophilic and eight conserved, highly hydrophobic beta-sheet regions of almost-equal-to 140 amino acids. These latter hydrophobic regions may be the CbpA domains that interact with the different enzymatic subunits of the cellulase complex.