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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Bibliographic Details
Published in:Protein science 2017-09, Vol.26 (9), p.1726-1737
Main Authors: Hammond, Robert G., Tan, Xuan, Johnson, Margaret A.
Format: Article
Language:English
Subjects:
Animals
Binding
Bioinformatics
Chiroptera
Coronaviridae
coronavirus
Coronavirus - chemistry
Coronaviruses
COVID-19
Deoxyribonucleic acid
DNA
double‐wing motif
Frataxin
Genomes
Models, Molecular
NMR
nonstructural protein
Nuclear magnetic resonance
Nuclear Magnetic Resonance, Biomolecular
Phylogeny
Protein Domains
Protein Folding
protein functional annotation
Protein interaction
Protein structure
Proteins
RNA-Dependent RNA Polymerase - chemistry
RNA-Dependent RNA Polymerase - metabolism
SARS‐unique domain
Severe acute respiratory syndrome
Severe acute respiratory syndrome-related coronavirus - chemistry
Transcription
Viral Nonstructural Proteins - chemistry
Viral Nonstructural Proteins - metabolism
viral protein
Viruses
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Description
Summary: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. PDB Code(s): 5UTV
ISSN:0961-8368
1469-896X
DOI:10.1002/pro.3208