6LSG

Crystal structure of the enterovirus 71 polymerase elongation complex (C0S6M form)

6LSG の概要

• エントリーDOI: 10.2210/pdb6lsg/pdb
• 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*A)-3'), ... (6 entities in total)
• 機能のキーワード: polymerase-rna complex, elongation, translocation intermediate, transferase-rna complex, transferase/rna
• 由来する生物種: Human enterovirus 71 (EV71); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 70031.83

構造登録者

Li, R.,Wang, M.,Jing, X.,Gong, P. (登録日: 2020-01-17, 公開日: 2020-04-29, 最終更新日: 2023-11-29)

主引用文献

Wang, M.,Li, R.,Shu, B.,Jing, X.,Ye, H.Q.,Gong, P.
Stringent control of the RNA-dependent RNA polymerase translocation revealed by multiple intermediate structures.
Nat Commun, 11:2605-2605, 2020

PubMed Abstract: Each polymerase nucleotide addition cycle is associated with two primary conformational changes of the catalytic complex: the pre-chemistry active site closure and post-chemistry translocation. While active site closure is well interpreted by numerous crystallographic snapshots, translocation intermediates are rarely captured. Here we report three types of intermediate structures in an RNA-dependent RNA polymerase (RdRP). The first two types, captured in forward and reverse translocation events, both highlight the role of RdRP-unique motif G in restricting the RNA template movement, corresponding to the rate-limiting step in translocation. By mutating two critical residues in motif G, we obtain the third type of intermediates that may mimic the transition state of this rate-limiting step, demonstrating a previously unidentified movement of the template strand. We propose that a similar strategy may be utilized by other classes of nucleic acid polymerases to ensure templating nucleotide positioning for efficient catalysis through restricting interactions with template RNA.

PubMed: 32451382
DOI: 10.1038/s41467-020-16234-4

実験手法

X-RAY DIFFRACTION (2.14 Å)