1 H, 13 C and 15 N backbone resonance assignment of the calcium-activated EndoU endoribonuclease

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...

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Bibliographic Details
Published in:Biomolecular NMR assignments 2024-12, Vol.18 (2), p.263
Main Authors: Malard, Florian, Karginov, Fedor V, Campagne, Sébastien
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Calcium - metabolism
Humans
Nitrogen Isotopes
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Secondary
Uridylate-Specific Endoribonucleases
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Summary: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.
ISSN:1874-270X