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DNA Sequence Recognition by DNA Primase Using High-Throughput Primase Profiling
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Structural analysis of the putative SARS-CoV-2 primase complex.

Eva Konkolova1, Martin Klima1, Radim Nencka1

  • 1Institute of Organic Chemistry and Biochemistry AS CR, v.v.i, Flemingovo nam. 2, 166 10 Prague 6, Czech Republic.

Journal of Structural Biology
|June 15, 2020
PubMed
Summary

The crystal structure of the SARS-CoV-2 primase (nsp7-nsp8 complex) reveals a heterotetramer. This structure highlights a potential RNA binding site crucial for viral replication.

Keywords:
Crystal structurePrimaseRNASARS-CoV-2

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Area of Science:

  • Structural Biology
  • Virology
  • Molecular Biology

Background:

  • The SARS-CoV-2 virus relies on various proteins for its replication cycle.
  • The nsp7 and nsp8 proteins are known components of the SARS-CoV-2 primase complex, essential for viral RNA synthesis.

Purpose of the Study:

  • To determine the high-resolution crystal structure of the SARS-CoV-2 putative primase.
  • To elucidate the quaternary structure and molecular interactions within the nsp7-nsp8 complex.

Main Methods:

  • X-ray crystallography was employed to obtain the crystal structure of the nsp7-nsp8 complex.
  • Structural analysis included identifying protein folds, interfaces, and surface electrostatic potentials.

Main Results:

  • The crystal structure revealed a heterotetrameric assembly (2:2 nsp7-nsp8) in the asymmetric unit.
  • A helical core formed by nsp7 and nsp8 is flanked by nsp8 β-sheet subdomains.
  • Hydrophobic interfaces mediate the assembly of the heterotetramer, with a significant interface area between nsp7 and nsp8.

Conclusions:

  • The determined structure provides detailed insights into the organization of the SARS-CoV-2 primase.
  • Analysis revealed a putative RNA binding site formed exclusively within the heterotetrameric complex, suggesting its functional importance.