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-基本情報
登録情報 | データベース: PDB / ID: 7ubk | ||||||
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タイトル | Transcription antitermination factor Qlambda, type-II crystal | ||||||
要素 | Antitermination protein Q | ||||||
キーワード | GENE REGULATION / RNA polymerase / DNA Binding / transcription / Q-dependent antitermination / Q antitermination factor | ||||||
機能・相同性 | 機能・相同性情報 transcription antitermination / DNA-templated transcription termination / DNA binding / zinc ion binding 類似検索 - 分子機能 | ||||||
生物種 | Escherichia phage Lambda (λファージ) | ||||||
手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 1.97 Å | ||||||
データ登録者 | Yin, Z. / Ebright, R.H. | ||||||
資金援助 | 米国, 1件
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引用 | ジャーナル: Proc Natl Acad Sci U S A / 年: 2022 タイトル: In transcription antitermination by Qλ, NusA induces refolding of Qλ to form a nozzle that extends the RNA polymerase RNA-exit channel. 著者: Zhou Yin / Jeremy G Bird / Jason T Kaelber / Bryce E Nickels / Richard H Ebright / 要旨: Lambdoid bacteriophage Q proteins are transcription antipausing and antitermination factors that enable RNA polymerase (RNAP) to read through pause and termination sites. Q proteins load onto RNAP ...Lambdoid bacteriophage Q proteins are transcription antipausing and antitermination factors that enable RNA polymerase (RNAP) to read through pause and termination sites. Q proteins load onto RNAP engaged in promoter-proximal pausing at a Q binding element (QBE) and adjacent sigma-dependent pause element to yield a Q-loading complex, and they translocate with RNAP as a pausing-deficient, termination-deficient Q-loaded complex. In previous work, we showed that the Q protein of bacteriophage 21 (Q21) functions by forming a nozzle that narrows and extends the RNAP RNA-exit channel, preventing formation of pause and termination RNA hairpins. Here, we report atomic structures of four states on the pathway of antitermination by the Q protein of bacteriophage λ (Qλ), a Q protein that shows no sequence similarity to Q21 and that, unlike Q21, requires the transcription elongation factor NusA for efficient antipausing and antitermination. We report structures of Qλ, the Qλ-QBE complex, the NusA-free pre-engaged Qλ-loading complex, and the NusA-containing engaged Qλ-loading complex. The results show that Qλ, like Q21, forms a nozzle that narrows and extends the RNAP RNA-exit channel, preventing formation of RNA hairpins. However, the results show that Qλ has no three-dimensional structural similarity to Q21, employs a different mechanism of QBE recognition than Q21, and employs a more complex process for loading onto RNAP than Q21, involving recruitment of Qλ to form a pre-engaged loading complex, followed by NusA-facilitated refolding of Qλ to form an engaged loading complex. The results establish that Qλ and Q21 are not structural homologs and are solely functional analogs. | ||||||
履歴 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 7ubk.cif.gz | 183.3 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb7ubk.ent.gz | 146.1 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 7ubk.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
文書・要旨 | 7ubk_validation.pdf.gz | 455.1 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 7ubk_full_validation.pdf.gz | 455.4 KB | 表示 | |
XML形式データ | 7ubk_validation.xml.gz | 13.4 KB | 表示 | |
CIF形式データ | 7ubk_validation.cif.gz | 17.5 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/ub/7ubk ftp://data.pdbj.org/pub/pdb/validation_reports/ub/7ubk | HTTPS FTP |
-関連構造データ
-リンク
-集合体
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非結晶学的対称性 (NCS) | NCSドメイン:
NCSドメイン領域: Ens-ID: 1
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