3OLB

Poliovirus polymerase elongation complex with 2',3'-dideoxy-ctp

3OLB の概要

• エントリーDOI: 10.2210/pdb3olb/pdb
• 分子名称: Polymerase, RNA (5'-R(*AP*AP*GP*UP*CP*U*CP*CP*AP*GP*GP*UP*CP*UP*CP*UP*CP*GP*UP*CP*CP*GP*GP*AP*AP*A)-3'), RNA (5'-R(*GP*CP*CP*CP*GP*GP*AP*CP*GP*AP*GP*AP*GP*A)-3'), ... (8 entities in total)
• 機能のキーワード: rna-dependent rna polymerase, elongation complex, virus, protein-rna complex, transferase-rna complex, transferase/rna
• 由来する生物種: Human poliovirus 1; 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 281106.76

構造登録者

Gong, P.,Peersen, O.B. (登録日: 2010-08-25, 公開日: 2010-12-22, 最終更新日: 2023-09-06)

主引用文献

Gong, P.,Peersen, O.B.
Structural basis for active site closure by the poliovirus RNA-dependent RNA polymerase.
Proc.Natl.Acad.Sci.USA, 107:22505-22510, 2010

PubMed Abstract: Positive-strand RNA viruses include a large number of human and animal pathogens whose essential RNA-dependent RNA polymerases (RdRPs) share a structurally homologous core with an encircled active site. RdRPs are targets for antiviral drug development, but these efforts are hindered by limited structural information about the RdRP catalytic cycle. To further our understanding of RdRP function, we assembled, purified, and then crystallized poliovirus elongation complexes after multiple rounds of nucleotide incorporation. Here we present structures capturing the active polymerase and its nucleotide triphosphate complexes in four distinct states, leading us to propose a six-state catalytic cycle involving residues that are highly conserved among positive-strand RNA virus RdRPs. The structures indicate that RdRPs use a fully prepositioned templating base for nucleotide recognition and close their active sites for catalysis using a novel structural rearrangement in the palm domain. The data also suggest that translocation by RDRPs may not be directly linked to the conformational changes responsible for active site closure and reopening.

PubMed: 21148772
DOI: 10.1073/pnas.1007626107

実験手法

X-RAY DIFFRACTION (2.41 Å)