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

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...

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Autores principales: Konkolova, Eva, Klima, Martin, Nencka, Radim, Boura, Evzen
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Inc. 2020
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7289108/
https://www.ncbi.nlm.nih.gov/pubmed/32535228
http://dx.doi.org/10.1016/j.jsb.2020.107548
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author Konkolova, Eva
Klima, Martin
Nencka, Radim
Boura, Evzen
author_facet Konkolova, Eva
Klima, Martin
Nencka, Radim
Boura, Evzen
author_sort Konkolova, Eva
collection PubMed
description 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 Å(2) connects the nsp7 to nsp8 and a second one of approx. 950 Å(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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spelling pubmed-72891082020-06-12 Structural analysis of the putative SARS-CoV-2 primase complex Konkolova, Eva Klima, Martin Nencka, Radim Boura, Evzen J Struct Biol Article 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 Å(2) connects the nsp7 to nsp8 and a second one of approx. 950 Å(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. Elsevier Inc. 2020-08-01 2020-06-11 /pmc/articles/PMC7289108/ /pubmed/32535228 http://dx.doi.org/10.1016/j.jsb.2020.107548 Text en © 2020 Elsevier Inc. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Konkolova, Eva
Klima, Martin
Nencka, Radim
Boura, Evzen
Structural analysis of the putative SARS-CoV-2 primase complex
title Structural analysis of the putative SARS-CoV-2 primase complex
title_full Structural analysis of the putative SARS-CoV-2 primase complex
title_fullStr Structural analysis of the putative SARS-CoV-2 primase complex
title_full_unstemmed Structural analysis of the putative SARS-CoV-2 primase complex
title_short Structural analysis of the putative SARS-CoV-2 primase complex
title_sort structural analysis of the putative sars-cov-2 primase complex
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7289108/
https://www.ncbi.nlm.nih.gov/pubmed/32535228
http://dx.doi.org/10.1016/j.jsb.2020.107548
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