Cargando…
The nsp9 Replicase Protein of SARS-Coronavirus, Structure and Functional Insights
As part of a high-throughput structural analysis of SARS-coronavirus (SARS-CoV) proteins, we have solved the structure of the non-structural protein 9 (nsp9). This protein, encoded by ORF1a, has no designated function but is most likely involved with viral RNA synthesis. The protein comprises a sing...
Autores principales: | , , , , , , , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cell Press. Published by Elsevier Ltd.
2004
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7135010/ https://www.ncbi.nlm.nih.gov/pubmed/14962394 http://dx.doi.org/10.1016/j.str.2004.01.016 |
_version_ | 1783517958649151488 |
---|---|
author | Sutton, Geoff Fry, Elizabeth Carter, Lester Sainsbury, Sarah Walter, Tom Nettleship, Joanne Berrow, Nick Owens, Ray Gilbert, Robert Davidson, Andrew Siddell, Stuart Poon, Leo L.M. Diprose, Jonathan Alderton, David Walsh, Martin Grimes, Jonathan M. Stuart, David I. |
author_facet | Sutton, Geoff Fry, Elizabeth Carter, Lester Sainsbury, Sarah Walter, Tom Nettleship, Joanne Berrow, Nick Owens, Ray Gilbert, Robert Davidson, Andrew Siddell, Stuart Poon, Leo L.M. Diprose, Jonathan Alderton, David Walsh, Martin Grimes, Jonathan M. Stuart, David I. |
author_sort | Sutton, Geoff |
collection | PubMed |
description | As part of a high-throughput structural analysis of SARS-coronavirus (SARS-CoV) proteins, we have solved the structure of the non-structural protein 9 (nsp9). This protein, encoded by ORF1a, has no designated function but is most likely involved with viral RNA synthesis. The protein comprises a single β-barrel with a fold previously unseen in single domain proteins. The fold superficially resembles an OB-fold with a C-terminal extension and is related to both of the two subdomains of the SARS-CoV 3C-like protease (which belongs to the serine protease superfamily). nsp9 has, presumably, evolved from a protease. The crystal structure suggests that the protein is dimeric. This is confirmed by analytical ultracentrifugation and dynamic light scattering. We show that nsp9 binds RNA and interacts with nsp8, activities that may be essential for its function(s). |
format | Online Article Text |
id | pubmed-7135010 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2004 |
publisher | Cell Press. Published by Elsevier Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71350102020-04-08 The nsp9 Replicase Protein of SARS-Coronavirus, Structure and Functional Insights Sutton, Geoff Fry, Elizabeth Carter, Lester Sainsbury, Sarah Walter, Tom Nettleship, Joanne Berrow, Nick Owens, Ray Gilbert, Robert Davidson, Andrew Siddell, Stuart Poon, Leo L.M. Diprose, Jonathan Alderton, David Walsh, Martin Grimes, Jonathan M. Stuart, David I. Structure Article As part of a high-throughput structural analysis of SARS-coronavirus (SARS-CoV) proteins, we have solved the structure of the non-structural protein 9 (nsp9). This protein, encoded by ORF1a, has no designated function but is most likely involved with viral RNA synthesis. The protein comprises a single β-barrel with a fold previously unseen in single domain proteins. The fold superficially resembles an OB-fold with a C-terminal extension and is related to both of the two subdomains of the SARS-CoV 3C-like protease (which belongs to the serine protease superfamily). nsp9 has, presumably, evolved from a protease. The crystal structure suggests that the protein is dimeric. This is confirmed by analytical ultracentrifugation and dynamic light scattering. We show that nsp9 binds RNA and interacts with nsp8, activities that may be essential for its function(s). Cell Press. Published by Elsevier Ltd. 2004-02 2004-02-25 /pmc/articles/PMC7135010/ /pubmed/14962394 http://dx.doi.org/10.1016/j.str.2004.01.016 Text en Copyright © 2004 Cell Press. Published by Elsevier Ltd. 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 Sutton, Geoff Fry, Elizabeth Carter, Lester Sainsbury, Sarah Walter, Tom Nettleship, Joanne Berrow, Nick Owens, Ray Gilbert, Robert Davidson, Andrew Siddell, Stuart Poon, Leo L.M. Diprose, Jonathan Alderton, David Walsh, Martin Grimes, Jonathan M. Stuart, David I. The nsp9 Replicase Protein of SARS-Coronavirus, Structure and Functional Insights |
title | The nsp9 Replicase Protein of SARS-Coronavirus, Structure and Functional Insights |
title_full | The nsp9 Replicase Protein of SARS-Coronavirus, Structure and Functional Insights |
title_fullStr | The nsp9 Replicase Protein of SARS-Coronavirus, Structure and Functional Insights |
title_full_unstemmed | The nsp9 Replicase Protein of SARS-Coronavirus, Structure and Functional Insights |
title_short | The nsp9 Replicase Protein of SARS-Coronavirus, Structure and Functional Insights |
title_sort | nsp9 replicase protein of sars-coronavirus, structure and functional insights |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7135010/ https://www.ncbi.nlm.nih.gov/pubmed/14962394 http://dx.doi.org/10.1016/j.str.2004.01.016 |
work_keys_str_mv | AT suttongeoff thensp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT fryelizabeth thensp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT carterlester thensp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT sainsburysarah thensp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT waltertom thensp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT nettleshipjoanne thensp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT berrownick thensp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT owensray thensp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT gilbertrobert thensp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT davidsonandrew thensp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT siddellstuart thensp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT poonleolm thensp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT diprosejonathan thensp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT aldertondavid thensp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT walshmartin thensp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT grimesjonathanm thensp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT stuartdavidi thensp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT suttongeoff nsp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT fryelizabeth nsp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT carterlester nsp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT sainsburysarah nsp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT waltertom nsp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT nettleshipjoanne nsp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT berrownick nsp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT owensray nsp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT gilbertrobert nsp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT davidsonandrew nsp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT siddellstuart nsp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT poonleolm nsp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT diprosejonathan nsp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT aldertondavid nsp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT walshmartin nsp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT grimesjonathanm nsp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights AT stuartdavidi nsp9replicaseproteinofsarscoronavirusstructureandfunctionalinsights |