6YHU
Crystal structure of the nsp7-nsp8 complex of SARS-CoV-2
Summary for 6YHU
Entry DOI | 10.2210/pdb6yhu/pdb |
Descriptor | Replicase polyprotein 1a (3 entities in total) |
Functional Keywords | nsp7, nsp8, sars-cov-2, ncov-2019, covid-19, viral protein |
Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) More |
Total number of polymer chains | 4 |
Total formula weight | 41636.16 |
Authors | Konkolova, E.,Klima, M.,Boura, E. (deposition date: 2020-03-31, release date: 2020-04-29, Last modification date: 2024-11-06) |
Primary citation | Konkolova, E.,Klima, M.,Nencka, R.,Boura, E. Structural analysis of the putative SARS-CoV-2 primase complex. J.Struct.Biol., 211:107548-107548, 2020 Cited by PubMed Abstract: 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 β-sheet subdomains. It was also revealed that two hydrophobic interfaces one of approx. 1340 Å connects the nsp7 to nsp8 and a second one of approx. 950 Å 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. PubMed: 32535228DOI: 10.1016/j.jsb.2020.107548 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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