5F8L

Enterovirus 71 Polymerase Elongation Complex (C3S1 Form)

5F8L の概要

• エントリーDOI: 10.2210/pdb5f8l/pdb
• 関連するPDBエントリー: 5F8G 5F8H 5F8I 5F8J 5F8M 5F8N 5F8O
• 分子名称: Genome polyprotein, RNA (35-MER), RNA (5'-R(*UP*GP*UP*UP*CP*GP*AP*CP*GP*AP*GP*AP*GP*AP*GP*AP*CP*C)-3'), ... (5 entities in total)
• 機能のキーワード: polymerase-rna complex, elongation, nucleotide addition cycle, transferase-rna complex, transferase/rna
• 由来する生物種: Enterovirus A71; 詳細
• 細胞内の位置: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Virion : E5RPG2
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 70518.08

構造登録者

Shu, B.,Gong, P. (登録日: 2015-12-09, 公開日: 2016-06-22, 最終更新日: 2023-11-08)

主引用文献

Shu, B.,Gong, P.
Structural basis of viral RNA-dependent RNA polymerase catalysis and translocation
Proc.Natl.Acad.Sci.USA, 113:E4005-E4014, 2016

PubMed Abstract: Viral RNA-dependent RNA polymerases (RdRPs) play essential roles in viral genome replication and transcription. We previously reported several structural states of the poliovirus RdRP nucleotide addition cycle (NAC) that revealed a unique palm domain-based active site closure mechanism and proposed a six-state NAC model including a hypothetical state representing translocation intermediates. Using the RdRP from another human enterovirus, enterovirus 71, here we report seven RdRP elongation complex structures derived from a crystal lattice that allows three NAC events. These structures suggested a key order of events in initial NTP binding and NTP-induced active site closure and revealed a bona fide translocation intermediate featuring asymmetric movement of the template-product duplex. Our work provides essential missing links in understanding NTP recognition and translocation mechanisms in viral RdRPs and emphasizes the uniqueness of the viral RdRPs compared with other processive polymerases.

PubMed: 27339134
DOI: 10.1073/pnas.1602591113

実験手法

X-RAY DIFFRACTION (2.812 Å)