脆弱拟杆菌纳米核糖核酸酶配体结合形式的晶体结构，属于 DHH/DHHA1 磷酸酯酶家族蛋白。
Crystal structure of the ligand-binding form of nanoRNase from Bacteroides fragilis, a member of the DHH/DHHA1 phosphoesterase family of proteins.
机构信息
Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka 565-0871, Japan.
出版信息
FEBS Lett. 2013 Aug 19;587(16):2669-74. doi: 10.1016/j.febslet.2013.06.053. Epub 2013 Jul 9.
Abstract
NanoRNase (Nrn) specifically degrades nucleoside 3',5'-bisphosphate and the very short RNA, nanoRNA, during the final step of mRNA degradation. The crystal structure of Nrn in complex with a reaction product GMP was determined. The overall structure consists of two domains that are interconnected by a flexible loop and form a cleft. Two Mn²⁺ ions are coordinated by conserved residues in the DHH motif of the N-terminal domain. GMP binds near the DHHA1 motif region in the C-terminal domain. Our structure enables us to predict the substrate-bound form of Nrn as well as other DHH/DHHA1 phosphoesterase family proteins.
摘要
纳米核糖核酸酶（Nrn）在 mRNA 降解的最后一步中特异性地降解核苷 3'，5'-二磷酸和非常短的 RNA，纳米 RNA。我们解析了 Nrn 与反应产物 GMP 形成的复合物的晶体结构。该结构整体由两个结构域组成，通过一个柔性环连接，并形成一个裂隙。两个 Mn²⁺离子由 N 端结构域的 DHH 基序中的保守残基配位。GMP 结合在 C 端结构域的 DHHA1 基序区域附近。我们的结构使我们能够预测 Nrn 以及其他 DHH/DHHA1 磷酸二酯酶家族蛋白的底物结合形式。
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