Summary information and primary citation
- PDB-id
- 3h5y; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- transferase-RNA
- Method
- X-ray (1.77 Å)
- Summary
- Norovirus polymerase+primer-template+ctp complex at 6 mm mncl2
- Reference
- Zamyatkin DF, Parra F, Machin A, Grochulski P, Ng KK (2009): "Binding of 2'-amino-2'-deoxycytidine-5'-triphosphate to norovirus polymerase induces rearrangement of the active site." J.Mol.Biol., 390, 10-16. doi: 10.1016/j.jmb.2009.04.069.
- Abstract
- Crystal structures of a genogroup II.4 human norovirus polymerase bound to an RNA primer-template duplex and the substrate analogue 2'-amino-2'-deoxycytidine-5'-triphosphate have been determined to 1.8 A resolution. The alteration of the substrate-binding site that is required to accommodate the 2'-amino group leads to a rearrangement of the polymerase active site and a disruption of the coordination shells of the active-site metal ions. The mode of binding seen for 2'-amino-2'-deoxycytidine-5'-triphosphate suggests a novel molecular mechanism of inhibition that may be exploited for the design of inhibitors targeting viral RNA polymerases.
