登録情報 データベース : EMDB / ID : EMD-4769 構造の表示 ダウンロードとリンクタイトル Cryo-EM structure of bacterial RNAP with a DNA mimic protein Ocr from T7 phage マップデータNone 詳細 試料複合体 : Structural basis of transcription inhibition by the DNA mimic Ocr protein of bacteriophage T7複合体 : DNA-directed RNA polymeraseタンパク質・ペプチド : DNA-directed RNA polymerase subunit alphaタンパク質・ペプチド : DNA-directed RNA polymerase subunit betaタンパク質・ペプチド : DNA-directed RNA polymerase subunit beta'タンパク質・ペプチド : DNA-directed RNA polymerase subunit omega複合体 : Ocr (Overcome classical restriction)タンパク質・ペプチド : Overcome classical restriction gp0.3 詳細機能・相同性 機能・相同性情報分子機能 ドメイン・相同性 構成要素
symbiont-mediated evasion of host restriction-modification system / RNA polymerase complex / submerged biofilm formation / cellular response to cell envelope stress / cytosolic DNA-directed RNA polymerase complex / regulation of DNA-templated transcription initiation / bacterial-type flagellum assembly / bacterial-type flagellum-dependent cell motility / nitrate assimilation / transcription elongation factor complex ... symbiont-mediated evasion of host restriction-modification system / RNA polymerase complex / submerged biofilm formation / cellular response to cell envelope stress / cytosolic DNA-directed RNA polymerase complex / regulation of DNA-templated transcription initiation / bacterial-type flagellum assembly / bacterial-type flagellum-dependent cell motility / nitrate assimilation / transcription elongation factor complex / regulation of DNA-templated transcription elongation / transcription antitermination / DNA-templated transcription initiation / cell motility / ribonucleoside binding / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / response to heat / protein-containing complex assembly / intracellular iron ion homeostasis / protein dimerization activity / response to antibiotic / virus-mediated perturbation of host defense response / DNA-templated transcription / magnesium ion binding / DNA binding / zinc ion binding / membrane / cytoplasm / cytosol 類似検索 - 分子機能 B-form DNA mimic Ocr / DNA mimic ocr / Protein Ocr / : / DNA-directed RNA polymerase, omega subunit / DNA-directed RNA polymerase, subunit beta-prime, bacterial type / DNA-directed RNA polymerase, beta subunit, external 1 domain superfamily / DNA-directed RNA polymerase, beta subunit, external 1 domain / RNA polymerase beta subunit external 1 domain / RNA polymerase, alpha subunit, C-terminal ... B-form DNA mimic Ocr / DNA mimic ocr / Protein Ocr / : / DNA-directed RNA polymerase, omega subunit / DNA-directed RNA polymerase, subunit beta-prime, bacterial type / DNA-directed RNA polymerase, beta subunit, external 1 domain superfamily / DNA-directed RNA polymerase, beta subunit, external 1 domain / RNA polymerase beta subunit external 1 domain / RNA polymerase, alpha subunit, C-terminal / Bacterial RNA polymerase, alpha chain C terminal domain / DNA-directed RNA polymerase, alpha subunit / DNA-directed RNA polymerase beta subunit, bacterial-type / RNA polymerase Rpb6 / RNA polymerase, subunit omega/Rpo6/RPB6 / RNA polymerase Rpb6 / RNA polymerase Rpb1, domain 3 superfamily / RNA polymerase Rpb1, clamp domain superfamily / RPB6/omega subunit-like superfamily / DNA-directed RNA polymerase, subunit beta-prime / RNA polymerase Rpb2, domain 2 superfamily / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 1 / RNA polymerase Rpb1, domain 1 / RNA polymerase, alpha subunit / RNA polymerase Rpb1, domain 4 / RNA polymerase Rpb1, domain 2 / RNA polymerase Rpb1, domain 4 / RNA polymerase, beta subunit, protrusion / RNA polymerase beta subunit / RNA polymerase, N-terminal / RNA polymerase Rpb1, funnel domain superfamily / RNA polymerase I subunit A N-terminus / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 5 / DNA-directed RNA polymerase, insert domain / DNA-directed RNA polymerase, RpoA/D/Rpb3-type / RNA polymerase Rpb3/RpoA insert domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerases D / DNA-directed RNA polymerase, insert domain superfamily / RNA polymerase, RBP11-like subunit / RNA polymerase Rpb2, domain 2 / RNA polymerase Rpb2, domain 2 / RNA polymerase, beta subunit, conserved site / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerase Rpb2, OB-fold / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerases beta chain signature. / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain / DNA-directed RNA polymerase, subunit 2 / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain superfamily / RNA polymerase Rpb2, domain 6 類似検索 - ドメイン・相同性 DNA-directed RNA polymerase subunit omega / Protein Ocr / DNA-directed RNA polymerase subunit alpha / DNA-directed RNA polymerase subunit omega / DNA-directed RNA polymerase subunit beta' / DNA-directed RNA polymerase subunit beta 類似検索 - 構成要素生物種 Escherichia coli K-12 (大腸菌) / Enterobacteria phage T7 (ファージ) / Escherichia coli (strain K12) (大腸菌)手法 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度 : 3.8 Å 詳細 データ登録者Ye FZ / Zhang XD 資金援助 英国, 1件 詳細 詳細を隠すOrganization Grant number 国 Biotechnology and Biological Sciences Research Council (BBSRC) BB/N007816 英国
引用ジャーナル : Elife / 年 : 2020タイトル : Structural basis of transcription inhibition by the DNA mimic protein Ocr of bacteriophage T7.著者 : Fuzhou Ye / Ioly Kotta-Loizou / Milija Jovanovic / Xiaojiao Liu / David Tf Dryden / Martin Buck / Xiaodong Zhang / 要旨 : Bacteriophage T7 infects and evades the host restriction/modification system. The Ocr protein of T7 was shown to exist as a dimer mimicking DNA and to bind to host restriction enzymes, thus ... Bacteriophage T7 infects and evades the host restriction/modification system. The Ocr protein of T7 was shown to exist as a dimer mimicking DNA and to bind to host restriction enzymes, thus preventing the degradation of the viral genome by the host. Here we report that Ocr can also inhibit host transcription by directly binding to bacterial RNA polymerase (RNAP) and competing with the recruitment of RNAP by sigma factors. Using cryo electron microscopy, we determined the structures of Ocr bound to RNAP. The structures show that an Ocr dimer binds to RNAP in the cleft, where key regions of sigma bind and where DNA resides during transcription synthesis, thus providing a structural basis for the transcription inhibition. Our results reveal the versatility of Ocr in interfering with host systems and suggest possible strategies that could be exploited in adopting DNA mimicry as a basis for forming novel antibiotics. 履歴 ヘッダ(付随情報) 公開 2018年6月6日 - 登録 2019年4月3日 - マップ公開 2020年2月26日 - 更新 2020年2月26日 - 現状 2020年2月26日 処理サイト : PDBe / 状態 : 公開
すべて表示 表示を減らす