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Structural analysis of the putative SARS-CoV-2 primase complex.

ABSTRACT: We report the crystal structure of the SARS-CoV-2 putative primase composed of the nsp7 and nsp8 proteins. We observed a dimer of dimers (2:2 nsp7-nsp8) in the crystallographic asymmetric unit. The structure revealed a fold with a helical core of the heterotetramer formed by both nsp7 and nsp8 that is flanked with two symmetry-related nsp8 ?-sheet subdomains. It was also revealed that two hydrophobic interfaces one of approx. 1340 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 connects the dimers and form the observed heterotetramer. Interestingly, analysis of the surface electrostatic potential revealed a putative RNA binding site that is formed only within the heterotetramer.

SUBMITTER: Konkolova E 

PROVIDER: S-EPMC7289108 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature

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Structural analysis of the putative SARS-CoV-2 primase complex.

Konkolova Eva E   Klima Martin M   Nencka Radim R   Boura Evzen E  

Journal of structural biology 20200611 2

We report the crystal structure of the SARS-CoV-2 putative primase composed of the nsp7 and nsp8 proteins. We observed a dimer of dimers (2:2 nsp7-nsp8) in the crystallographic asymmetric unit. The structure revealed a fold with a helical core of the heterotetramer formed by both nsp7 and nsp8 that is flanked with two symmetry-related nsp8 β-sheet subdomains. It was also revealed that two hydrophobic interfaces one of approx. 1340 Å<sup>2</sup> connects the nsp7 to nsp8 and a second one of appro  ...[more]

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