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  • Structural analysis of the putative SARS-CoV-2 primase complex #MMPMID32535228
  • Konkolova E; Klima M; Nencka R; Boura E
  • J Struct Biol 2020[Aug]; 211 (2): 107548 PMID32535228show ga
  • We report the crystal structure of the SARS-CoV-2 putative primase composed of the nsp7 and nsp8 proteins. We observed a dimer of dimers (2:2 nsp7-nsp8) in the crystallographic asymmetric unit. The structure revealed a fold with a helical core of the heterotetramer formed by both nsp7 and nsp8 that is flanked with two symmetry-related nsp8 beta-sheet subdomains. It was also revealed that two hydrophobic interfaces one of approx. 1340 A(2) connects the nsp7 to nsp8 and a second one of approx. 950 A(2) connects the dimers and form the observed heterotetramer. Interestingly, analysis of the surface electrostatic potential revealed a putative RNA binding site that is formed only within the heterotetramer.
  • |Betacoronavirus/*chemistry[MESH]
  • |Binding Sites[MESH]
  • |Coronavirus RNA-Dependent RNA Polymerase[MESH]
  • |Crystallography, X-Ray[MESH]
  • |DNA Primase/*chemistry/metabolism[MESH]
  • |Models, Molecular[MESH]
  • |Multiprotein Complexes[MESH]
  • |Protein Conformation[MESH]
  • |Protein Multimerization[MESH]
  • |RNA/metabolism[MESH]
  • |SARS-CoV-2[MESH]
  • |Viral Nonstructural Proteins/*chemistry/metabolism[MESH]

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  • suck abstract from ncbi

    107548 2.211 2020