嗜热栖热菌tRNase Z柔性臂的结构与同源酶的结构不同。
The structure of the flexible arm of Thermotoga maritima tRNase Z differs from those of homologous enzymes.
作者信息
Ishii Ryohei, Minagawa Asako, Takaku Hiroaki, Takagi Masamichi, Nashimoto Masayuki, Yokoyama Shigeyuki
机构信息
RIKEN Genomic Sciences Center, Tsurumi, Yokohama 230-0045, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt 8):637-41. doi: 10.1107/S1744309107033623. Epub 2007 Jul 21.
tRNA 3'-processing endoribonuclease (tRNase Z) is one of the enzymes involved in the 3'-end processing of precursor tRNAs and is a member of the metallo-beta-lactamase superfamily. tRNase Z crystal structures have revealed that the enzyme forms a dimer and has a characteristic domain, named a flexible arm or an exosite, which protrudes from the metallo-beta-lactamase core and is involved in tRNA binding. The refined structure of Thermotoga maritima tRNase Z has been determined at 1.97 A resolution, revealing the structure of the flexible arm and the zinc-bound active site. The structure of the flexible arm of T. maritima tRNase Z is distinct from those of the Bacillus subtilis and Escherichia coli tRNase Zs. A comparison of the three tRNase Z structures revealed differences in the dimer orientation, which may be related to the unique cleavage-site specificity of T. maritima tRNase Z.
tRNA 3'-加工内切核糖核酸酶（tRNase Z）是参与前体tRNA 3'-末端加工的酶之一，属于金属β-内酰胺酶超家族成员。tRNase Z晶体结构显示该酶形成二聚体，并有一个特征性结构域，称为柔性臂或别构部位，它从金属β-内酰胺酶核心突出并参与tRNA结合。嗜热栖热菌tRNase Z的精细结构已在1.97 Å分辨率下确定，揭示了柔性臂和锌结合活性位点的结构。嗜热栖热菌tRNase Z柔性臂的结构与枯草芽孢杆菌和大肠杆菌tRNase Z的结构不同。对这三种tRNase Z结构的比较揭示了二聚体取向的差异，这可能与嗜热栖热菌tRNase Z独特的切割位点特异性有关。
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