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 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.
Structural analysis of the putative SARS-CoV-2 primase complex
E. Konkoľová,M. Klíma,Radim Nencka,E. Bouřa
Published 2020 in Journal of Structural Biology
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- Publication year
2020
- Venue
Journal of Structural Biology
- Publication date
2020-06-11
- Fields of study
Medicine, Chemistry
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Semantic Scholar, PubMed
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