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钙激活的内EndoU 内切核酸酶的 H、C 和 N 骨架共振赋值。

H, C and N backbone resonance assignment of the calcium-activated EndoU endoribonuclease.

机构信息

Univ. Bordeaux, CNRS, INSERM, ARNA, UMR 5320, U1212, Bordeaux, F-33000, France.

Univ. Bordeaux, CNRS, INSERM, IECB, US1, UAR 3033, Pessac, F-33600, France.

出版信息

Biomol NMR Assign. 2024 Dec;18(2):263-267. doi: 10.1007/s12104-024-10198-y. Epub 2024 Sep 9.

Abstract

The catalytic domain of the calcium-dependent endoribonuclease EndoU from Homo sapiens was expressed in E. coli with C and N labeling. A nearly complete assignment of backbone H, N, and C resonances was obtained, as well as a secondary structure prediction based on the assigned chemical shifts. The predicted secondary structures were almost identical to the published crystal structure of calcium-activated EndoU. This is the first NMR study of an eukaryotic member of the EndoU-like superfamily of ribonucleases.

摘要

人源钙离子依赖型内切核酸酶 EndoU 的催化结构域在大肠杆菌中进行 C 和 N 标记表达。获得了近乎完整的 H、N 和 C 骨架共振信号分配,以及基于分配的化学位移的二级结构预测。预测的二级结构与已发表的钙激活 EndoU 晶体结构几乎完全一致。这是对 EndoU 样 RNA 酶超家族中真核成员的首次 NMR 研究。

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