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10.1016/j.jsb.2020.107548 http://scihub22266oqcxt.onion/10.1016/j.jsb.2020.107548 32535228!7289108!32535228     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Struct+Biol 2020 ; 211 (2): 107548 Nephropedia Template TP {{tp|p=32535228|t=2020. Structural analysis of the putative SARS-CoV-2 primase complex |pdf=|usr=}}{{32535228}} gab.com Text Structural analysis of the putative SARS-CoV-2 primase complex JO: J Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=32535228 #FOAvip 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. Twit Text FOAVip Structural analysis of the putative SARS-CoV-2 primase complex ????J Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=32535228 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32535228 #FOAvip English Wikipedia <ref>{{Cite pmid|32535228}}</ref> 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]Structural analysis of the putative SARS-CoV-2 primase complex (epmc).pdf DeepDyve Pubget Overpricing