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Refolding of lid subdomain of SARS-CoV-2 nsp14 upon nsp10 interaction releases exonuclease activity.
Structure 30, 1050-1054.e2 (2022)
Publ. Version/Full Text
Research data
DOI
PMC
During RNA replication, coronaviruses require proofreading to maintain the integrity of their large genomes. Nsp14 associates with viral polymerase complex to excise the mismatched nucleotides. Aside from the exonuclease activity, nsp14 methyltransferase domain mediates cap methylation, facilitating translation initiation and protecting viral RNA from recognition by the innate immune sensors. The nsp14 exonuclease activity is modulated by a protein co-factor nsp10. While the nsp10/nsp14 complex structure is available, the mechanistic basis for nsp10-mediated modulation remains unclear in the absence of the nsp14 structure. Here, we provide a crystal structure of nsp14 in an apo-form. Comparative analysis of the apo- and nsp10-bound structures explain the modulatory role of the co-factor protein and reveal the allosteric nsp14 control mechanism essential for drug discovery. Further, the flexibility of the N-terminal lid of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) nsp14 structure presented in this study rationalizes the recently proposed idea of nsp14/nsp10/nsp16 ternary complex.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Sah ; Sars-cov-2 ; Xrd ; Coronavirus ; Methylation ; Methyltransferase ; Nsp10 ; Nsp14 ; Proof-reading ; Structure
ISSN (print) / ISBN
0969-2126
e-ISSN
1878-4186
Journal
Structure
Quellenangaben
Volume: 30,
Issue: 8,
Pages: 1050-1054.e2
Publisher
Cell Press
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)