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

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

Publication date: Jun 11, 2020

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 A connects the nsp7 to nsp8 and a second one of approx. 950 A 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.

Concepts Keywords
Asymmetric Unit Primase
Crystal DNA replication
Dimer SARS
Dimers Dimer
Electrostatic Potential
Helical
Hydrophobic
Primase
SARS
Symmetry

Original Article

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