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.
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页数：6
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