Structural analysis of the putative SARS-CoV-2 primase complex
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...
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| Autor*in: |
Konkolova, Eva [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2020transfer abstract |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Hormuz salt distribution in the United Arab Emirates: Implications for the location of hydrocarbon fields - Geng, Meixia ELSEVIER, 2022, San Diego, Calif |
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| Übergeordnetes Werk: |
volume:211 ; year:2020 ; number:2 ; day:1 ; month:08 ; pages:0 |
| Links: |
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| DOI / URN: |
10.1016/j.jsb.2020.107548 |
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ELV050783491 |
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| 520 | |a 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 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 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. | ||
| 520 | |a 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 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 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. | ||
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10.1016/j.jsb.2020.107548 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001059.pica (DE-627)ELV050783491 (ELSEVIER)S1047-8477(20)30121-0 DE-627 ger DE-627 rakwb eng 550 VZ 38.48 bkl 38.51 bkl Konkolova, Eva verfasserin aut Structural analysis of the putative SARS-CoV-2 primase complex 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 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. 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 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 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. SARS-CoV-2 Elsevier RNA Elsevier Primase Elsevier Crystal structure Elsevier Klima, Martin oth Nencka, Radim oth Boura, Evzen oth Enthalten in Elsevier Geng, Meixia ELSEVIER Hormuz salt distribution in the United Arab Emirates: Implications for the location of hydrocarbon fields 2022 San Diego, Calif (DE-627)ELV008286124 volume:211 year:2020 number:2 day:1 month:08 pages:0 https://doi.org/10.1016/j.jsb.2020.107548 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 38.48 Marine Geologie VZ 38.51 Geologie fossiler Brennstoffe VZ AR 211 2020 2 1 0801 0 |
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10.1016/j.jsb.2020.107548 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001059.pica (DE-627)ELV050783491 (ELSEVIER)S1047-8477(20)30121-0 DE-627 ger DE-627 rakwb eng 550 VZ 38.48 bkl 38.51 bkl Konkolova, Eva verfasserin aut Structural analysis of the putative SARS-CoV-2 primase complex 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 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. 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 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 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. SARS-CoV-2 Elsevier RNA Elsevier Primase Elsevier Crystal structure Elsevier Klima, Martin oth Nencka, Radim oth Boura, Evzen oth Enthalten in Elsevier Geng, Meixia ELSEVIER Hormuz salt distribution in the United Arab Emirates: Implications for the location of hydrocarbon fields 2022 San Diego, Calif (DE-627)ELV008286124 volume:211 year:2020 number:2 day:1 month:08 pages:0 https://doi.org/10.1016/j.jsb.2020.107548 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 38.48 Marine Geologie VZ 38.51 Geologie fossiler Brennstoffe VZ AR 211 2020 2 1 0801 0 |
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10.1016/j.jsb.2020.107548 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001059.pica (DE-627)ELV050783491 (ELSEVIER)S1047-8477(20)30121-0 DE-627 ger DE-627 rakwb eng 550 VZ 38.48 bkl 38.51 bkl Konkolova, Eva verfasserin aut Structural analysis of the putative SARS-CoV-2 primase complex 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 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. 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 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 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. SARS-CoV-2 Elsevier RNA Elsevier Primase Elsevier Crystal structure Elsevier Klima, Martin oth Nencka, Radim oth Boura, Evzen oth Enthalten in Elsevier Geng, Meixia ELSEVIER Hormuz salt distribution in the United Arab Emirates: Implications for the location of hydrocarbon fields 2022 San Diego, Calif (DE-627)ELV008286124 volume:211 year:2020 number:2 day:1 month:08 pages:0 https://doi.org/10.1016/j.jsb.2020.107548 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 38.48 Marine Geologie VZ 38.51 Geologie fossiler Brennstoffe VZ AR 211 2020 2 1 0801 0 |
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10.1016/j.jsb.2020.107548 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001059.pica (DE-627)ELV050783491 (ELSEVIER)S1047-8477(20)30121-0 DE-627 ger DE-627 rakwb eng 550 VZ 38.48 bkl 38.51 bkl Konkolova, Eva verfasserin aut Structural analysis of the putative SARS-CoV-2 primase complex 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 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. 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 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 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. SARS-CoV-2 Elsevier RNA Elsevier Primase Elsevier Crystal structure Elsevier Klima, Martin oth Nencka, Radim oth Boura, Evzen oth Enthalten in Elsevier Geng, Meixia ELSEVIER Hormuz salt distribution in the United Arab Emirates: Implications for the location of hydrocarbon fields 2022 San Diego, Calif (DE-627)ELV008286124 volume:211 year:2020 number:2 day:1 month:08 pages:0 https://doi.org/10.1016/j.jsb.2020.107548 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 38.48 Marine Geologie VZ 38.51 Geologie fossiler Brennstoffe VZ AR 211 2020 2 1 0801 0 |
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10.1016/j.jsb.2020.107548 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001059.pica (DE-627)ELV050783491 (ELSEVIER)S1047-8477(20)30121-0 DE-627 ger DE-627 rakwb eng 550 VZ 38.48 bkl 38.51 bkl Konkolova, Eva verfasserin aut Structural analysis of the putative SARS-CoV-2 primase complex 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier 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 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 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. 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 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 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. SARS-CoV-2 Elsevier RNA Elsevier Primase Elsevier Crystal structure Elsevier Klima, Martin oth Nencka, Radim oth Boura, Evzen oth Enthalten in Elsevier Geng, Meixia ELSEVIER Hormuz salt distribution in the United Arab Emirates: Implications for the location of hydrocarbon fields 2022 San Diego, Calif (DE-627)ELV008286124 volume:211 year:2020 number:2 day:1 month:08 pages:0 https://doi.org/10.1016/j.jsb.2020.107548 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-GGO 38.48 Marine Geologie VZ 38.51 Geologie fossiler Brennstoffe VZ AR 211 2020 2 1 0801 0 |
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550 VZ 38.48 bkl 38.51 bkl Structural analysis of the putative SARS-CoV-2 primase complex SARS-CoV-2 Elsevier RNA Elsevier Primase Elsevier Crystal structure Elsevier |
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Hormuz salt distribution in the United Arab Emirates: Implications for the location of hydrocarbon fields |
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Hormuz salt distribution in the United Arab Emirates: Implications for the location of hydrocarbon fields |
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Structural analysis of the putative SARS-CoV-2 primase complex |
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Structural analysis of the putative SARS-CoV-2 primase complex |
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Konkolova, Eva |
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Hormuz salt distribution in the United Arab Emirates: Implications for the location of hydrocarbon fields |
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Hormuz salt distribution in the United Arab Emirates: Implications for the location of hydrocarbon fields |
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10.1016/j.jsb.2020.107548 |
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structural analysis of the putative sars-cov-2 primase complex |
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Structural analysis of the putative SARS-CoV-2 primase complex |
| 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 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 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. |
| abstractGer |
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 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 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. |
| abstract_unstemmed |
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 Å2 connects the nsp7 to nsp8 and a second one of approx. 950 Å2 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. |
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Structural analysis of the putative SARS-CoV-2 primase complex |
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Klima, Martin Nencka, Radim Boura, Evzen |
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