Structural analysis of the putative SARS-CoV-2 primase complex.
J Struct Biol
; 211(2): 107548, 2020 08 01.
Article
in English
| MEDLINE | ID: covidwho-593332
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 (22 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 ß-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.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Viral Nonstructural Proteins
/
DNA Primase
/
Betacoronavirus
Language:
English
Journal:
J Struct Biol
Journal subject:
Molecular Biology
Year:
2020
Document Type:
Article
Affiliation country:
J.jsb.2020.107548
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