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首页> 外文期刊>EMBO Journal >Crystal structure of a eukaryote/archaeon-like prolyl-tRNA synthetase and its complex with tRNA(Pro)(CGG)
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Crystal structure of a eukaryote/archaeon-like prolyl-tRNA synthetase and its complex with tRNA(Pro)(CGG)

机译：晶体结构的真核生物/ archaeon-likeprolyl-tRNA合成酶及其复杂

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摘要

Prolyl-tRNA synthetase (ProRS) is a class IIa synthetase that, according to sequence analysis, occurs in different organisms with one of two quite distinct structural architectures: prokaryote-like and eukaryote/archaeon-like, The primary sequence of ProRS from the hypothermophilic eubacterium Thermus thermophilus (ProRSTT) shows that this enzyme is surprisingly eukaryote/archaeon-like We describe its crystal structure at 2.43 (A) over circle resolution, which reveals a feature that is unique among class II synthetases. This is an additional zinc-containing domain after the expected class IIa anticodon-binding domain and whose C-terminal extremity, which ends in an absolutely conserved tyrosine, folds back into the active site. We also present an improved structure of ProRSTT complexed with tRNA(PRO)(CGG) at 2.85 Angstrom resolution. This structure represents an initial docking state of the tRNA in which the anticodon stem-loop is engaged, particularly via the tRNA(PRO)-specific bases G35 and G36, but the 3' end does not enter the active site. Considerable structural changes in tRNA and/or synthetase, which are probably induced by small substrates, are required to achieve the conformation active for aminoacylation. [References: 43]
机译：Prolyl-tRNA合成酶(ProRS)是一个类活动花絮合成酶,根据序列分析,发生在两种不同的生物截然不同的结构体系结构:prokaryote-like和真核生物/ archaeon-like,主要的ProRS序列hypothermophilic真细菌栖热菌属酸奶(ProRSTT)表明,这种酶是惊人的真核生物/ archaeon-like我们描述其晶体结构分辨率2.43 (A)圈,这揭示了一个特性,是独一无二的二类合成酶。zinc-containing域后预期的类花絮anticodon-binding域,其c端肢体,以绝对守恒的酪氨酸,折叠回活性部位。还提供了一个提高ProRSTT结构包裹着tRNA (PRO) (CGG) 2.85埃决议。对接的tRNA反密码子茎环结构订婚了,特别是通过tRNA (PRO)特殊G35基地和产品G36,但3 '结束不进入活性部位。的结构性变化tRNA和/或合成酶,这可能是由小的基板,需要实现构象活跃氨酰化。

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