Structural characterization of endoribonuclease Nsp15 from SARS CoV-2
نویسندگان
چکیده
منابع مشابه
Mutational analysis of the SARS virus Nsp15 endoribonuclease: identification of residues affecting hexamer formation.
The severe acute respiratory syndrome (SARS) coronavirus virus non-structural protein 15 is a Mn2+-dependent endoribonuclease with specificity for cleavage at uridylate residues. To better understand structural and functional characteristics of Nsp15, 22 mutant versions of Nsp15 were produced in Escherichia coli as His-tagged proteins and purified by metal-affinity and ion-exchange chromatograp...
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متن کاملThe severe acute respiratory syndrome coronavirus Nsp15 protein is an endoribonuclease that prefers manganese as a cofactor.
Nonstructural protein 15 (Nsp15) of the severe acute respiratory syndrome coronavirus (SARS-CoV) produced in Escherichia coli has endoribonuclease activity that preferentially cleaved 5' of uridylates of RNAs. Blocking either the 5' or 3' terminus did not affect cleavage. Double- and single-stranded RNAs were both substrates for Nsp15 but with different kinetics for cleavage. Mn(2+) at 2 to 10 ...
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ژورنال
عنوان ژورنال: Acta Crystallographica
سال: 2021
ISSN: ['2053-2733']
DOI: https://doi.org/10.1107/s0108767321089078