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3MMP

Structure of the Qb replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins

3MMP の概要
エントリーDOI10.2210/pdb3mmp/pdb
分子名称Elongation factor Tu 2, Elongation factor Ts, RNA-directed RNA polymerase beta chain, (2S)-1-[3-{[(2R)-2-hydroxypropyl]oxy}-2,2-bis({[(2R)-2-hydroxypropyl]oxy}methyl)propoxy]propan-2-ol, ... (4 entities in total)
機能のキーワードrdrp, host-factor complex, translation, transferase
由来する生物種Escherichia coli
詳細
細胞内の位置Cytoplasm: P0CE48
タンパク質・核酸の鎖数4
化学式量合計279836.80
構造登録者
Kidmose, R.T.,Vasiliev, N.N.,Chetverin, A.B.,Knudsen, C.R.,Andersen, G.R. (登録日: 2010-04-20, 公開日: 2010-06-09, 最終更新日: 2023-09-06)
主引用文献Kidmose, R.T.,Vasiliev, N.N.,Chetverin, A.B.,Andersen, G.R.,Knudsen, C.R.
Structure of the Qbeta replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins.
Proc.Natl.Acad.Sci.USA, 107:10884-10889, 2010
Cited by
PubMed Abstract: The RNA-dependent RNA polymerase core complex formed upon infection of Escherichia coli by the bacteriophage Qbeta is composed of the viral catalytic beta-subunit as well as the host translation elongation factors EF-Tu and EF-Ts, which are required for initiation of RNA replication. We have determined the crystal structure of the complex between the beta-subunit and the two host proteins to 2.5-A resolution. Whereas the basic catalytic machinery in the viral subunit appears similar to other RNA-dependent RNA polymerases, a unique C-terminal region of the beta-subunit engages in extensive interactions with EF-Tu and may contribute to the separation of the transient duplex formed between the template and the nascent product to allow exponential amplification of the phage genome. The evolution of resistance by the host appears to be impaired because of the interactions of the beta-subunit with parts of EF-Tu essential in recognition of aminoacyl-tRNA.
PubMed: 20534494
DOI: 10.1073/pnas.1003015107
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 3mmp
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2026-04-15に公開中

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