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10.1038/s41467-020-19662-4 http://scihub22266oqcxt.onion/10.1038/s41467-020-19662-4 33208735!7674412!33208735     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2020 ; 11 (1): 5877 Nephropedia Template TP {{tp|p=33208735|t=2020. Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site |pdf=|usr=}}{{33208735}} gab.com Text Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=33208735 #FOAvip Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), the pathogen that causes the disease COVID-19, produces replicase polyproteins 1a and 1ab that contain, respectively, 11 or 16 nonstructural proteins (nsp). Nsp5 is the main protease (M(pro)) responsible for cleavage at eleven positions along these polyproteins, including at its own N- and C-terminal boundaries, representing essential processing events for subsequent viral assembly and maturation. We have determined X-ray crystallographic structures of this cysteine protease in its wild-type free active site state at 1.8 A resolution, in its acyl-enzyme intermediate state with the native C-terminal autocleavage sequence at 1.95 A resolution and in its product bound state at 2.0 A resolution by employing an active site mutation (C145A). We characterize the stereochemical features of the acyl-enzyme intermediate including critical hydrogen bonding distances underlying catalysis in the Cys/His dyad and oxyanion hole. We also identify a highly ordered water molecule in a position compatible for a role as the deacylating nucleophile in the catalytic mechanism and characterize the binding groove conformational changes and dimerization interface that occur upon formation of the acyl-enzyme. Collectively, these crystallographic snapshots provide valuable mechanistic and structural insights for future antiviral therapeutic development including revised molecular docking strategies based on M(pro) inhibition. Twit Text FOAVip Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=33208735 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33208735 #FOAvip English Wikipedia <ref>{{Cite pmid|33208735}}</ref> Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site #MMPMID33208735 Lee J; Worrall LJ; Vuckovic M; Rosell FI; Gentile F; Ton AT; Caveney NA; Ban F; Cherkasov A; Paetzel M; Strynadka NCJ Nat Commun 2020[Nov]; 11 (1): 5877 PMID33208735show ga Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), the pathogen that causes the disease COVID-19, produces replicase polyproteins 1a and 1ab that contain, respectively, 11 or 16 nonstructural proteins (nsp). Nsp5 is the main protease (M(pro)) responsible for cleavage at eleven positions along these polyproteins, including at its own N- and C-terminal boundaries, representing essential processing events for subsequent viral assembly and maturation. We have determined X-ray crystallographic structures of this cysteine protease in its wild-type free active site state at 1.8 A resolution, in its acyl-enzyme intermediate state with the native C-terminal autocleavage sequence at 1.95 A resolution and in its product bound state at 2.0 A resolution by employing an active site mutation (C145A). We characterize the stereochemical features of the acyl-enzyme intermediate including critical hydrogen bonding distances underlying catalysis in the Cys/His dyad and oxyanion hole. We also identify a highly ordered water molecule in a position compatible for a role as the deacylating nucleophile in the catalytic mechanism and characterize the binding groove conformational changes and dimerization interface that occur upon formation of the acyl-enzyme. Collectively, these crystallographic snapshots provide valuable mechanistic and structural insights for future antiviral therapeutic development including revised molecular docking strategies based on M(pro) inhibition. |Betacoronavirus/chemistry/*enzymology[MESH] |Binding Sites[MESH] |Catalytic Domain[MESH] |Coronavirus 3C Proteases[MESH] |Crystallography, X-Ray[MESH] |Cysteine Endopeptidases/*chemistry/genetics/metabolism[MESH] |Dimerization[MESH] |Humans[MESH] |Models, Molecular[MESH] |Mutation[MESH] |Protease Inhibitors/metabolism[MESH] |Protein Conformation[MESH] |SARS-CoV-2[MESH] |Substrate Specificity[MESH]Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-(epmc).pdf DeepDyve Pubget Overpricing