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

被引：51

作者：

Konkolova, Eva ^{[1
]}

Klima, Martin ^{[1
]}

Nencka, Radim ^{[1
]}

Boura, Evzen ^{[1
]}

机构：

[1] Inst Organ Chem & Biochem AS CR, Vvi, Flemingovo Nam 2, Prague 16610 6, Czech Republic

来源：

JOURNAL OF STRUCTURAL BIOLOGY | 2020年 / 211卷 / 02期

关键词：

SARS-CoV-2; RNA; Primase; Crystal structure; RNA-POLYMERASE; CORONAVIRUS; DELTACORONAVIRUS; GAMMACORONAVIRUS; REPLICATION; DISCOVERY;

D O I：

10.1016/j.jsb.2020.107548

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 beta-sheet subdomains. It was also revealed that two hydrophobic interfaces one of approx. 1340 angstrom(2) connects the nsp7 to nsp8 and a second one of approx. 950 angstrom(2) 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.

引用

页数：6

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