Advanced

Crystal Structure of Non-Structural Protein 10 from Severe Acute Respiratory Syndrome Coronavirus-2

Rogstam, Annika LU ; Nyblom, Maria LU ; Christensen, Signe LU ; Sele, Celeste LU ; Talibov, Vladimir O LU ; Lindvall, Therese LU ; Rasmussen, Anna Andersson LU ; André, Ingemar LU ; Fisher, Zoë LU and Knecht, Wolfgang LU , et al. (2020) In International Journal of Molecular Sciences 21(19).
Abstract

Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2), causing Coronavirus Disease 19 (COVID-19), emerged at the end of 2019 and quickly spread to cause a global pandemic with severe socio-economic consequences. The early sequencing of its RNA genome revealed its high similarity to SARS, likely to have originated from bats. The SARS-CoV-2 non-structural protein 10 (nsp10) displays high sequence similarity with its SARS homologue, which binds to and stimulates the 3'-to-5' exoribonuclease and the 2'-O-methlytransferase activities of nsps 14 and 16, respectively. Here, we report the biophysical characterization and 1.6 Å resolution structure of the unbound form of nsp10 from SARS-CoV-2 and compare it to the structures of its SARS... (More)

Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2), causing Coronavirus Disease 19 (COVID-19), emerged at the end of 2019 and quickly spread to cause a global pandemic with severe socio-economic consequences. The early sequencing of its RNA genome revealed its high similarity to SARS, likely to have originated from bats. The SARS-CoV-2 non-structural protein 10 (nsp10) displays high sequence similarity with its SARS homologue, which binds to and stimulates the 3'-to-5' exoribonuclease and the 2'-O-methlytransferase activities of nsps 14 and 16, respectively. Here, we report the biophysical characterization and 1.6 Å resolution structure of the unbound form of nsp10 from SARS-CoV-2 and compare it to the structures of its SARS homologue and the complex-bound form with nsp16 from SARS-CoV-2. The crystal structure and solution behaviour of nsp10 will not only form the basis for understanding the role of SARS-CoV-2 nsp10 as a central player of the viral RNA capping apparatus, but will also serve as a basis for the development of inhibitors of nsp10, interfering with crucial functions of the replication-transcription complex and virus replication.

(Less)
Please use this url to cite or link to this publication:
author
; ; ; ; ; ; ; ; and , et al. (More)
; ; ; ; ; ; ; ; ; and (Less)
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
International Journal of Molecular Sciences
volume
21
issue
19
article number
7375
pages
15 pages
publisher
MDPI AG
external identifiers
  • scopus:85092227602
  • pmid:33036230
ISSN
1422-0067
DOI
10.3390/ijms21197375
language
English
LU publication?
yes
id
9b21ff9c-37cc-4e50-8a2b-f241b4ce9d5a
date added to LUP
2020-10-12 13:14:17
date last changed
2021-02-28 05:35:28
@article{9b21ff9c-37cc-4e50-8a2b-f241b4ce9d5a,
  abstract     = {<p>Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2), causing Coronavirus Disease 19 (COVID-19), emerged at the end of 2019 and quickly spread to cause a global pandemic with severe socio-economic consequences. The early sequencing of its RNA genome revealed its high similarity to SARS, likely to have originated from bats. The SARS-CoV-2 non-structural protein 10 (nsp10) displays high sequence similarity with its SARS homologue, which binds to and stimulates the 3'-to-5' exoribonuclease and the 2'-O-methlytransferase activities of nsps 14 and 16, respectively. Here, we report the biophysical characterization and 1.6 Å resolution structure of the unbound form of nsp10 from SARS-CoV-2 and compare it to the structures of its SARS homologue and the complex-bound form with nsp16 from SARS-CoV-2. The crystal structure and solution behaviour of nsp10 will not only form the basis for understanding the role of SARS-CoV-2 nsp10 as a central player of the viral RNA capping apparatus, but will also serve as a basis for the development of inhibitors of nsp10, interfering with crucial functions of the replication-transcription complex and virus replication.</p>},
  author       = {Rogstam, Annika and Nyblom, Maria and Christensen, Signe and Sele, Celeste and Talibov, Vladimir O and Lindvall, Therese and Rasmussen, Anna Andersson and André, Ingemar and Fisher, Zoë and Knecht, Wolfgang and Kozielski, Frank},
  issn         = {1422-0067},
  language     = {eng},
  month        = {10},
  number       = {19},
  publisher    = {MDPI AG},
  series       = {International Journal of Molecular Sciences},
  title        = {Crystal Structure of Non-Structural Protein 10 from Severe Acute Respiratory Syndrome Coronavirus-2},
  url          = {http://dx.doi.org/10.3390/ijms21197375},
  doi          = {10.3390/ijms21197375},
  volume       = {21},
  year         = {2020},
}