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1H, 13C and 15N backbone chemical shift assignments of SARS-CoV-2 nsp3a.

ABSTRACT: The non-structural protein nsp3 from SARS-CoV-2 plays an essential role in the viral replication transcription complex. Nsp3a constitutes the N-terminal domain of nsp3, comprising a ubiquitin-like folded domain and a disordered acidic chain. This region of nsp3a has been linked to interactions with the viral nucleoprotein and the structure of double membrane vesicles. Here, we report the backbone resonance assignment of both domains of nsp3a. The study is carried out in the context of the international covid19-nmr consortium, which aims to characterize SARS-CoV-2 proteins and RNAs, providing for example NMR chemical shift assignments of the different viral components. Our assignment will provide the basis for the identification of inhibitors and further functional and interaction studies of this essential protein.

SUBMITTER: Salvi N 

PROVIDER: S-EPMC7819138 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature

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<sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N backbone chemical shift assignments of SARS-CoV-2 nsp3a.

Salvi Nicola N   Bessa Luiza Mamigonian LM   Guseva Serafima S   Camacho-Zarco Aldo A   Maurin Damien D   Perez Laura Marino LM   Malki Anas A   Hengesbach Martin M   Korn Sophie Marianne SM   Schlundt Andreas A   Schwalbe Harald H   Blackledge Martin M  

Biomolecular NMR assignments 20210121 1

The non-structural protein nsp3 from SARS-CoV-2 plays an essential role in the viral replication transcription complex. Nsp3a constitutes the N-terminal domain of nsp3, comprising a ubiquitin-like folded domain and a disordered acidic chain. This region of nsp3a has been linked to interactions with the viral nucleoprotein and the structure of double membrane vesicles. Here, we report the backbone resonance assignment of both domains of nsp3a. The study is carried out in the context of the intern  ...[more]

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