3BSO
Norwalk Virus polymerase bound to cytidine 5'-triphosphate and primer-template RNA
Summary for 3BSO
| Entry DOI | 10.2210/pdb3bso/pdb |
| Related | 1SH0 3BSN |
| Descriptor | RNA dependent RNA polymerase, RNA (5'-R(*UP*GP*CP*CP*CP*GP*GP*G)-3'), RNA (5'-R(P*UP*GP*CP*CP*CP*GP*GP*GP*C)-3'), ... (7 entities in total) |
| Functional Keywords | rna-dependent rna polymerase, viral replication, antiviral enzyme inhibitor, helicase, hydrolase, nucleotide-binding, nucleotidyltransferase, rna replication, rna-directed rna polymerase, transferase, transferase-rna complex, transferase/rna |
| Biological source | Norwalk virus More |
| Total number of polymer chains | 3 |
| Total formula weight | 63280.26 |
| Authors | Zamyatkin, D.F.,Ng, K.K.S. (deposition date: 2007-12-26, release date: 2008-01-08, Last modification date: 2024-02-21) |
| Primary citation | Zamyatkin, D.F.,Parra, F.,Alonso, J.M.,Harki, D.A.,Peterson, B.R.,Grochulski, P.,Ng, K.K. Structural insights into mechanisms of catalysis and inhibition in norwalk virus polymerase. J.Biol.Chem., 283:7705-7712, 2008 Cited by PubMed Abstract: Crystal structures of Norwalk virus polymerase bound to an RNA primer-template duplex and either the natural substrate CTP or the inhibitor 5-nitrocytidine triphosphate have been determined to 1.8A resolution. These structures reveal a closed conformation of the polymerase that differs significantly from previously determined open structures of calicivirus and picornavirus polymerases. These closed complexes are trapped immediately prior to the nucleotidyl transfer reaction, with the triphosphate group of the nucleotide bound to two manganese ions at the active site, poised for reaction to the 3'-hydroxyl group of the RNA primer. The positioning of the 5-nitrocytidine triphosphate nitro group between the alpha-phosphate and the 3'-hydroxyl group of the primer suggests a novel, general approach for the design of antiviral compounds mimicking natural nucleosides and nucleotides. PubMed: 18184655DOI: 10.1074/jbc.M709563200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
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