3H5Y
Norovirus polymerase+primer/template+CTP complex at 6 mM MnCl2
3H5Y の概要
エントリーDOI | 10.2210/pdb3h5y/pdb |
関連するPDBエントリー | 1SH0 3BSN 3BSO 3H5X |
分子名称 | 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) |
機能のキーワード | caliciviruses, viral rna polymerase, hydrolase, nucleotide-binding, nucleotidyltransferase, protease, rna replication, rna-directed rna polymerase, thiol protease, transferase, transferase-rna complex, transferase/rna |
由来する生物種 | Norwalk virus 詳細 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 63335.19 |
構造登録者 | Zamyatkin, D.F.,Parra, F.,Machin, A.,Grochulski, P.,Ng, K.K.S. (登録日: 2009-04-22, 公開日: 2009-05-19, 最終更新日: 2023-09-06) |
主引用文献 | 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 Cited by 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: 19426741DOI: 10.1016/j.jmb.2009.04.069 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.77 Å) |
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