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SARS‐unique fold in the Rousettus bat coronavirus HKU9

The coronavirus nonstructural protein 3 (nsp3) is a multifunctional protein that comprises multiple structural domains. This protein assists viral polyprotein cleavage, host immune interference, and may play other roles in genome replication or transcription. Here, we report the solution NMR structu...

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Detalles Bibliográficos
Autores principales: Hammond, Robert G., Tan, Xuan, Johnson, Margaret A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5563143/
https://www.ncbi.nlm.nih.gov/pubmed/28580734
http://dx.doi.org/10.1002/pro.3208
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author Hammond, Robert G.
Tan, Xuan
Johnson, Margaret A.
author_facet Hammond, Robert G.
Tan, Xuan
Johnson, Margaret A.
author_sort Hammond, Robert G.
collection PubMed
description The coronavirus nonstructural protein 3 (nsp3) is a multifunctional protein that comprises multiple structural domains. This protein assists viral polyprotein cleavage, host immune interference, and may play other roles in genome replication or transcription. Here, we report the solution NMR structure of a protein from the “SARS‐unique region” of the bat coronavirus HKU9. The protein contains a frataxin fold or double‐wing motif, which is an α + β fold that is associated with protein/protein interactions, DNA binding, and metal ion binding. High structural similarity to the human severe acute respiratory syndrome (SARS) coronavirus nsp3 is present. A possible functional site that is conserved among some betacoronaviruses has been identified using bioinformatics and biochemical analyses. This structure provides strong experimental support for the recent proposal advanced by us and others that the “SARS‐unique” region is not unique to the human SARS virus, but is conserved among several different phylogenetic groups of coronaviruses and provides essential functions.
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spelling pubmed-55631432018-09-01 SARS‐unique fold in the Rousettus bat coronavirus HKU9 Hammond, Robert G. Tan, Xuan Johnson, Margaret A. Protein Sci Articles The coronavirus nonstructural protein 3 (nsp3) is a multifunctional protein that comprises multiple structural domains. This protein assists viral polyprotein cleavage, host immune interference, and may play other roles in genome replication or transcription. Here, we report the solution NMR structure of a protein from the “SARS‐unique region” of the bat coronavirus HKU9. The protein contains a frataxin fold or double‐wing motif, which is an α + β fold that is associated with protein/protein interactions, DNA binding, and metal ion binding. High structural similarity to the human severe acute respiratory syndrome (SARS) coronavirus nsp3 is present. A possible functional site that is conserved among some betacoronaviruses has been identified using bioinformatics and biochemical analyses. This structure provides strong experimental support for the recent proposal advanced by us and others that the “SARS‐unique” region is not unique to the human SARS virus, but is conserved among several different phylogenetic groups of coronaviruses and provides essential functions. John Wiley and Sons Inc. 2017-06-15 2017-09 /pmc/articles/PMC5563143/ /pubmed/28580734 http://dx.doi.org/10.1002/pro.3208 Text en © 2017 The Protein Society
spellingShingle Articles
Hammond, Robert G.
Tan, Xuan
Johnson, Margaret A.
SARS‐unique fold in the Rousettus bat coronavirus HKU9
title SARS‐unique fold in the Rousettus bat coronavirus HKU9
title_full SARS‐unique fold in the Rousettus bat coronavirus HKU9
title_fullStr SARS‐unique fold in the Rousettus bat coronavirus HKU9
title_full_unstemmed SARS‐unique fold in the Rousettus bat coronavirus HKU9
title_short SARS‐unique fold in the Rousettus bat coronavirus HKU9
title_sort sars‐unique fold in the rousettus bat coronavirus hku9
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5563143/
https://www.ncbi.nlm.nih.gov/pubmed/28580734
http://dx.doi.org/10.1002/pro.3208
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