3H5Y

Norovirus polymerase+primer/template+CTP complex at 6 mM MnCl2

Summary for 3H5Y

• Entry DOI: 10.2210/pdb3h5y/pdb
• Related: 1SH0 3BSN 3BSO 3H5X
• Descriptor: RNA dependent RNA polymerase, 5'-R(*UP*GP*CP*CP*CP*GP*GP*G)-3', 5'-R(P*UP*GP*CP*CP*CP*GP*GP*GP*C)-3', ... (7 entities in total)
• Functional Keywords: caliciviruses, viral rna polymerase, hydrolase, nucleotide-binding, nucleotidyltransferase, protease, rna replication, rna-directed rna polymerase, thiol protease, transferase, transferase-rna complex, transferase/rna
• Biological source: Norwalk virus; More
• Total number of polymer chains: 3
• Total formula weight: 63335.19

Authors

Zamyatkin, D.F.,Parra, F.,Machin, A.,Grochulski, P.,Ng, K.K.S. (deposition date: 2009-04-22, release date: 2009-05-19, Last modification date: 2023-09-06)

Primary citation

Zamyatkin, D.F.,Parra, F.,Machin, A.,Grochulski, P.,Ng, K.K.
Binding of 2'-amino-2'-deoxycytidine-5'-triphosphate to norovirus polymerase induces rearrangement of the active site.
J.Mol.Biol., 390:10-16, 2009

PubMed 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.

PubMed: 19426741
DOI: 10.1016/j.jmb.2009.04.069

Experimental method

X-RAY DIFFRACTION (1.77 Å)