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10.1038/s41467-020-19770-1 http://scihub22266oqcxt.onion/10.1038/s41467-020-19770-1 33208736!7675986!33208736     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2020 ; 11 (1): 5874 Nephropedia Template TP {{tp|p=33208736|t=2020. Architecture of a SARS-CoV-2 mini replication and transcription complex |pdf=|usr=}}{{33208736}} gab.com Text Architecture of a SARS-CoV-2 mini replication and transcription complex JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=33208736 #FOAvip Non-structural proteins (nsp) constitute the SARS-CoV-2 replication and transcription complex (RTC) to play a pivotal role in the virus life cycle. Here we determine the atomic structure of a SARS-CoV-2 mini RTC, assembled by viral RNA-dependent RNA polymerase (RdRp, nsp12) with a template-primer RNA, nsp7 and nsp8, and two helicase molecules (nsp13-1 and nsp13-2), by cryo-electron microscopy. Two groups of mini RTCs with different conformations of nsp13-1 are identified. In both of them, nsp13-1 stabilizes overall architecture of the mini RTC by contacting with nsp13-2, which anchors the 5'-extension of RNA template, as well as interacting with nsp7-nsp8-nsp12-RNA. Orientation shifts of nsp13-1 results in its variable interactions with other components in two forms of mini RTC. The mutations on nsp13-1:nsp12 and nsp13-1:nsp13-2 interfaces prohibit the enhancement of helicase activity achieved by mini RTCs. These results provide an insight into how helicase couples with polymerase to facilitate its function in virus replication and transcription. Twit Text FOAVip Architecture of a SARS-CoV-2 mini replication and transcription complex ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=33208736 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33208736 #FOAvip English Wikipedia <ref>{{Cite pmid|33208736}}</ref> Architecture of a SARS-CoV-2 mini replication and transcription complex #MMPMID33208736 Yan L; Zhang Y; Ge J; Zheng L; Gao Y; Wang T; Jia Z; Wang H; Huang Y; Li M; Wang Q; Rao Z; Lou Z Nat Commun 2020[Nov]; 11 (1): 5874 PMID33208736show ga Non-structural proteins (nsp) constitute the SARS-CoV-2 replication and transcription complex (RTC) to play a pivotal role in the virus life cycle. Here we determine the atomic structure of a SARS-CoV-2 mini RTC, assembled by viral RNA-dependent RNA polymerase (RdRp, nsp12) with a template-primer RNA, nsp7 and nsp8, and two helicase molecules (nsp13-1 and nsp13-2), by cryo-electron microscopy. Two groups of mini RTCs with different conformations of nsp13-1 are identified. In both of them, nsp13-1 stabilizes overall architecture of the mini RTC by contacting with nsp13-2, which anchors the 5'-extension of RNA template, as well as interacting with nsp7-nsp8-nsp12-RNA. Orientation shifts of nsp13-1 results in its variable interactions with other components in two forms of mini RTC. The mutations on nsp13-1:nsp12 and nsp13-1:nsp13-2 interfaces prohibit the enhancement of helicase activity achieved by mini RTCs. These results provide an insight into how helicase couples with polymerase to facilitate its function in virus replication and transcription. |*Virus Replication[MESH] |Betacoronavirus/*chemistry/genetics/metabolism/*physiology[MESH] |Binding Sites[MESH] |Cryoelectron Microscopy[MESH] |Humans[MESH] |Methyltransferases/chemistry/genetics/metabolism[MESH] |Models, Molecular[MESH] |Mutation[MESH] |Protein Binding[MESH] |Protein Conformation[MESH] |RNA Helicases/chemistry/genetics/metabolism[MESH] |RNA, Viral/metabolism[MESH] |SARS-CoV-2[MESH] |Structure-Activity Relationship[MESH] |Transcription, Genetic[MESH]Architecture of a SARS-CoV-2 mini replication and transcription comple(epmc).pdf DeepDyve Pubget Overpricing