7XD9

Crystal Structure of Dengue Virus serotype 2 (DENV2) Polymerase Elongation Complex (CTP Form)

7XD9 の概要

• エントリーDOI: 10.2210/pdb7xd9/pdb
• 分子名称: NS5, RNA (30-mer), RNA (9-mer), ... (8 entities in total)
• 機能のキーワード: rna-dependent rna polymerase, de novo synthesis, elongation complex, priming element, transferase, transferase-rna complex, transferase/rna
• 由来する生物種: Dengue virus 2; 詳細
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 530757.71

構造登録者

Wu, J.,Wang, X.,Gong, P. (登録日: 2022-03-26, 公開日: 2022-12-21, 最終更新日: 2023-11-29)

主引用文献

Wu, J.,Wang, X.,Liu, Q.,Lu, G.,Gong, P.
Structural basis of transition from initiation to elongation in de novo viral RNA-dependent RNA polymerases.
Proc.Natl.Acad.Sci.USA, 120:e2211425120-e2211425120, 2023

PubMed Abstract: De novo viral RNA-dependent RNA polymerases (RdRPs) utilize their priming element (PE) to facilitate accurate initiation. Upon transition to elongation, the PE has to retreat from the active site to give room to the template-product RNA duplex. However, PE conformational change upon this transition and the role of PE at elongation both remain elusive. Here, we report crystal structures of RdRP elongation complex (EC) from dengue virus serotype 2 (DENV2), demonstrating a dramatic refolding of PE that allows establishment of interactions with the RNA duplex backbone approved to be essential for EC stability. Enzymology data from both DENV2 and hepatitis C virus (HCV) RdRPs suggest that critical transition of the refolding likely occurs after synthesis of a 4- to 5-nucleotide (nt) product together providing a key basis in understanding viral RdRP transition from initiation to elongation.

PubMed: 36577062
DOI: 10.1073/pnas.2211425120

実験手法

X-RAY DIFFRACTION (2.58 Å)