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1UVM

The structural basis for RNA specificity and Ca2 inhibition of an RNA-dependent RNA polymerase phi6p2 with 5NT RNA conformation A

1UVM の概要
エントリーDOI10.2210/pdb1uvm/pdb
関連するPDBエントリー1HHS 1HHT 1HI0 1HI1 1HI8 1UVI 1UVJ 1UVK 1UVL 1UVN
分子名称RNA-directed RNA polymerase, 5'-R(*UP*UP*UP*CP*CP)-3', MANGANESE (II) ION, ... (4 entities in total)
機能のキーワードpolymerase, transferase, nucleotidyltransferase, transcription
由来する生物種Pseudomonas phage phi6 (Bacteriophage phi-6)
詳細
細胞内の位置Virion: P11124
タンパク質・核酸の鎖数6
化学式量合計229326.14
構造登録者
Salgado, P.S.,Makeyev, E.V.,Butcher, S.,Bamford, D.,Stuart, D.I.,Grimes, J.M. (登録日: 2004-01-21, 公開日: 2004-02-19, 最終更新日: 2023-12-13)
主引用文献Salgado, P.S.,Makeyev, E.V.,Butcher, S.J.,Bamford, D.H.,Stuart, D.I.,Grimes, J.M.
The structural basis for RNA specificity and Ca2+ inhibition of an RNA-dependent RNA polymerase.
Structure, 12:307-316, 2004
Cited by
PubMed Abstract: The RNA-dependent RNA polymerase of bacteriophage phi6 transcribes mRNA from the three segments of the dsRNA viral genome. We have cocrystallized RNA oligonucleotides with the polymerase, revealing the mode of binding of RNA templates. This binding is somewhat different from that previously seen for DNA oligomers, leading to additional RNA-protein hydrogen bonds, consistent with a preference for RNA. Activation of the RNA/polymerase complex by the addition of substrate and Mg2+ initiates a single round of reaction within the crystal to form a dead-end complex that partially collapses within the enzyme active site. By replacing Mg2+ with Ca2+, we have been able to capture the inhibited complex which shows distortion that explains the structural basis for the inhibition of such polymerases by Ca2+.
PubMed: 14962391
DOI: 10.1016/j.str.2004.01.012
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 1uvm
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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