tRNA (Pro)反密码子识别栖热菌属酸奶prolyl-tRNA合成酶。

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库萨克年代,Yaremchuk, Krikliviy我Tukalo M

tRNA (Pro)反密码子识别栖热菌属酸奶prolyl-tRNA合成酶。

结构。1998年1月15日,6 (1):101 - 8。

PubMed ID

9493271 (在PubMed

]

文摘

背景:大多数氨酰合成酶(aar)专门识别全部或部分的反密码子的核苷酸三联体同源图示。IIb类活动花絮和类aar具有结构独特的tRNA anticodon-binding域。IIb类酶(LysRS AspRS和AsnRS)有一个氨基端beta-barrel域(OB-fold);这个域的相互作用与反密码子茎环结构为AspRS和LysRS为特征。四,五类活动花絮酶(ProRS、ThrRS HisRS GlyRS,但不是SerRS)有一个c端anticodon-binding域α/β折叠,没有找到任何其他蛋白质。RNA结合的模式这一领域是迄今为止未知的理由,如果有的话,后面的分类为不同的aar anticodon-binding域。结果:晶体结构的栖热菌属酸奶prolyl-tRNA合成酶(ProRSTT)在复杂的tRNA (Pro) 3.5分辨率取决于分子替换使用本机酶结构。tRNA分子,只有较低的三分之二的命令,发现绑定到合成酶二聚体。c端anticodon-binding域绑定到主要的反密码子茎环槽的一面。绑定的tRNA ProRSTT让人想起IIb类酶之间的相互作用与同源图示,但只有三个anticodon-loop基地成为张开第35 - 37(基地),而不是五(基地33-37)IIb类的酶。 The two anticodon bases conserved in all tRNA(Pro), G35 and G36, are specifically recognised by ProRSTT. CONCLUSIONS: For the synthetases possessing the class IIa anticodon-binding domain (ProRS, ThrRS and GlyRS, with the exception of HisRS), the two anticodon bases 35 and 36 are sufficient to uniquely identify the cognate tRNA (GG for proline, GU for threonine, CC for glycine), because these amino acids occupy full codon groups. The structure of ProRSTT in complex with its cognate tRNA shows that these two bases specifically interact with the enzyme, whereas base 34, which can be any base, is stacked under base 33 and makes no interactions with the synthetase. This is in agreement with biochemical experiments which identify bases 35 and 36 as major tRNA identity elements. In contrast, class IIb synthetases (AspRS, AsnRS and LysRS) have a distinct anticodon-binding domain that specifically recognises all three anticodon bases. This again correlates with the requirements of the genetic code for cognate tRNA identification, as the class IIb amino acids occupy half codon groups.

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药物靶点

药物	目标	类	生物	药理作用	行动
苏氨酸	苏氨酸——tRNA连接酶,胞质	蛋白质	人类	未知的	不可用	细节