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Revealing the Structural Plasticity of SARS-CoV-2 nsp7 and nsp8 Using Structural Proteomics (HDX-MS)

ABSTRACT: SARS-CoV-2 nsp7 and nsp8 are important cofactors of the RTC, as they interact and regulate the activity of RNA-dependent RNA polymerase and other nspsHere we used solution-based structural proteomic techniques, hydrogen-deuterium exchange mass spectrometry (HDX-MS) and crosslinking mass spectrometry (XL-MS), illuminate the dynamics of SARS-CoV-2 full-length nsp7, nsp8, and nsp7:nsp8 proteins and protein complex.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Severe Acute Respiratory Syndrome Coronavirus 2

SUBMITTER: Valentine Courouble

LAB HEAD: Patrick Griffin

PROVIDER: PXD026066 | Pride | 2022-01-12

REPOSITORIES: Pride

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			Action	DRS
	HDXreport_nsp7vnsp7nsp81to1.csv	Csv
	HDXreport_nsp7vnsp7nsp81to3.csv	Csv
	HDXreport_nsp8vnsp7nsp81to1.csv	Csv
	HDXreport_nsp8vnsp7nsp83to1.csv	Csv
	nsp7_10_1.raw	Raw

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Publications

Revealing the Structural Plasticity of SARS-CoV-2 nsp7 and nsp8 Using Structural Proteomics.

Courouble Valentine V VV Dey Sanjay Kumar SK Yadav Ruchi R Timm Jennifer J Harrison Jerry Joe E K JJEK Ruiz Francesc X FX Arnold Eddy E Griffin Patrick R PR

Journal of the American Society for Mass Spectrometry 20210614 7

Coronavirus (CoV) nonstructural proteins (nsps) assemble to form the replication-transcription complex (RTC) responsible for viral RNA synthesis. nsp7 and nsp8 are important cofactors of the RTC, as they interact and regulate the activity of RNA-dependent RNA polymerase and other nsps. To date, no structure of the full-length SARS-CoV-2 nsp7:nsp8 complex has been published. The current understanding of this complex is based on structures from truncated constructs, with missing electron densities ...[more]

PMID: 34121407

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