Disordered C-terminal domain of tyrosyl-tRNA synthetase: Secondary structure prediction
Disordered C-terminal domain of tyrosyl-tRNA synthetase: Secondary structure prediction
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DOI：
10.1016/s0300-9084(99)80057-1
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发表时间：
1999-03-01
期刊：
影响因子：
3.9
通讯作者：
Bedouelle, H
中科院分区：
文献类型：
--
作者：
Jermutus, L;Guez, V;Bedouelle, H
嗜热脂肪芽孢杆菌酪氨酰-tRNA合成酶（TyrRS）的C-末端结构域（残基320-419）在晶体结构中是无序的，并且参与tRNA（Tyr）的反密码子臂的结合。对11个原核或线粒体来源的TyrRS序列进行了比对，比对结果显示C-末端结构域序列中存在保守残基。一个共识可以推断出从应用程序的二级结构预测的查询集的11个序列。这些结果表明，C-末端结构域的序列决定了一个精确和保守的二级结构。他们预测C末端结构域将具有混合折叠（α/β或α + β），其中α螺旋位于序列的前半部分，β链主要位于序列的后半部分。应用了几个单独从序列识别折叠的程序，通过线程连接到已知结构上，但它们都没有识别出查询集的不同序列所共有的折叠类型。因此，折叠的C-末端，反密码子结合域可能是新的。(C)法国生物化学与分子生物学协会/爱思唯尔，巴黎。
The C-terminal domain (residues 320-419) of tyrosyl-tRNA synthetase (TyrRS) from Bacillus stearothermophilus is disordered in the crystal structure and involved in the binding of the anticodon arm of tRNA(Tyr). The sequences of 11 TyrRSs of prokaryotic or mitochondrial origins were aligned and the alignment showed the existence of conserved residues in the sequences of the C-terminal domains. A consensus could be deduced from the application of five programs of secondary structure prediction to the 11 sequences of the query set. These results suggested that the sequences of the C-terminal domains determined a precise and conserved secondary structure. They predicted that the C-terminal domain would have a mixed fold (alpha/beta or alpha+beta), with the alpha-helices in the first half of the sequence and the beta-strands mainly in its second half. Several programs of fold recognition from sequence alone, by threading onto known structures, were applied but none of them identified a type of fold that would be common to the different sequences of the query set. Therefore, the fold of the C-terminal, anticodon binding domain might be novel. (C) Societe francaise de biochimie et biologie moleculaire / Elsevier, Paris.