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Updated: Jun 13, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
Published on: November 1, 2024
1H, 13C and 15N backbone resonance assignment of the calcium-activated EndoU endoribonuclease
Florian Malard1,2, Fedor V Karginov3, Sébastien Campagne4,5
1Univ. Bordeaux, CNRS, INSERM, ARNA, UMR 5320, U1212, Bordeaux, F-33000, France. florian.malard@gmail.com.
Abstract:
The catalytic domain of the calcium-dependent endoribonuclease EndoU from Homo sapiens was expressed in E. coli with 13C and 15N labeling. A nearly complete assignment of backbone 1H, 15N, and 13C 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.
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