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10.1038/s41467-020-16234-4 http://scihub22266oqcxt.onion/10.1038/s41467-020-16234-4 32451382!7248106!32451382     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2020 ; 11 (1): 2605 Nephropedia Template TP {{tp|p=32451382|t=2020. Stringent control of the RNA-dependent RNA polymerase translocation revealed by multiple intermediate structures |pdf=|usr=}}{{32451382}} gab.com Text Stringent control of the RNA-dependent RNA polymerase translocation revealed by multiple intermediate structures JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32451382 #FOAvip Each polymerase nucleotide addition cycle is associated with two primary conformational changes of the catalytic complex: the pre-chemistry active site closure and post-chemistry translocation. While active site closure is well interpreted by numerous crystallographic snapshots, translocation intermediates are rarely captured. Here we report three types of intermediate structures in an RNA-dependent RNA polymerase (RdRP). The first two types, captured in forward and reverse translocation events, both highlight the role of RdRP-unique motif G in restricting the RNA template movement, corresponding to the rate-limiting step in translocation. By mutating two critical residues in motif G, we obtain the third type of intermediates that may mimic the transition state of this rate-limiting step, demonstrating a previously unidentified movement of the template strand. We propose that a similar strategy may be utilized by other classes of nucleic acid polymerases to ensure templating nucleotide positioning for efficient catalysis through restricting interactions with template RNA. Twit Text FOAVip Stringent control of the RNA-dependent RNA polymerase translocation revealed by multiple intermediate structures ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=32451382 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32451382 #FOAvip English Wikipedia <ref>{{Cite pmid|32451382}}</ref> Stringent control of the RNA-dependent RNA polymerase translocation revealed by multiple intermediate structures #MMPMID32451382 Wang M; Li R; Shu B; Jing X; Ye HQ; Gong P Nat Commun 2020[May]; 11 (1): 2605 PMID32451382show ga Each polymerase nucleotide addition cycle is associated with two primary conformational changes of the catalytic complex: the pre-chemistry active site closure and post-chemistry translocation. While active site closure is well interpreted by numerous crystallographic snapshots, translocation intermediates are rarely captured. Here we report three types of intermediate structures in an RNA-dependent RNA polymerase (RdRP). The first two types, captured in forward and reverse translocation events, both highlight the role of RdRP-unique motif G in restricting the RNA template movement, corresponding to the rate-limiting step in translocation. By mutating two critical residues in motif G, we obtain the third type of intermediates that may mimic the transition state of this rate-limiting step, demonstrating a previously unidentified movement of the template strand. We propose that a similar strategy may be utilized by other classes of nucleic acid polymerases to ensure templating nucleotide positioning for efficient catalysis through restricting interactions with template RNA. |Amino Acid Motifs[MESH] |Amino Acid Sequence[MESH] |Amino Acid Substitution[MESH] |Base Sequence[MESH] |Biological Transport, Active[MESH] |Catalytic Domain[MESH] |Crystallography, X-Ray[MESH] |Enterovirus A, Human/enzymology/genetics[MESH] |Genes, Viral[MESH] |Humans[MESH] |Models, Molecular[MESH] |Mutagenesis, Site-Directed[MESH] |Nucleic Acid Conformation[MESH] |Protein Conformation[MESH] |RNA, Viral/chemistry/genetics/metabolism[MESH] |RNA-Dependent RNA Polymerase/*chemistry/genetics/*metabolism[MESH] |Transcription Elongation, Genetic[MESH]Stringent control of the RNA-dependent RNA polymerase translocation re(epmc).pdf DeepDyve Pubget Overpricing