登録情報 データベース : EMDB / ID : EMD-4890 構造の表示 ダウンロードとリンクタイトル Structure of Vaccinia Virus DNA-dependent RNA polymerase co-transcriptional capping complex マップデータPost-processed cryo-EM map. 詳細 試料複合体 : Vaccinia Virus DNA-dependent RNA polymerase co-transcriptional capping complex複合体 : DNA-dependent RNA polymerase subunit RNAポリメラーゼ複合体 : RNA リボ核酸複合体 : syntheticリガンド : x 3種 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
ポリヌクレオチド-5'-ホスファターゼ / DNA-templated viral transcription / inorganic triphosphate phosphatase activity / virion component => GO:0044423 / mRNA 5'-triphosphate monophosphatase activity / mRNA 5'-phosphatase / polynucleotide 5'-phosphatase activity / viral transcription / RNA polymerase I activity / RNA polymerase II activity ... ポリヌクレオチド-5'-ホスファターゼ / DNA-templated viral transcription / inorganic triphosphate phosphatase activity / virion component => GO:0044423 / mRNA 5'-triphosphate monophosphatase activity / mRNA 5'-phosphatase / polynucleotide 5'-phosphatase activity / viral transcription / RNA polymerase I activity / RNA polymerase II activity / DNA-directed RNA polymerase complex / virion component / DNA-templated transcription termination / ribonucleoside binding / DNA-directed 5'-3' RNA polymerase activity / ポリメラーゼ / mRNA guanylyltransferase activity / mRNA guanylyltransferase / mRNA (guanine-N7)-methyltransferase / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / DNA-templated transcription / GTP binding / DNA binding / RNA binding / zinc ion binding / metal ion binding 類似検索 - 分子機能 mRNA-capping enzyme catalytic subunit, OB fold domain superfamily / mRNA-capping enzyme catalytic subunit, nucleotidyltransferase domain superfamily / mRNA-capping enzyme catalytic subunit, RNA triphosphatase domain superfamily / : / : / mRNA capping enzyme catalytic subunit, GTase, NTPase domain / mRNA-capping enzyme catalytic subunit, GTase, OB fold / Poxvirus mRNA capping enzyme, small subunit / Poxvirus mRNA capping enzyme, small subunit superfamily / Poxvirus mRNA capping enzyme, small subunit ... mRNA-capping enzyme catalytic subunit, OB fold domain superfamily / mRNA-capping enzyme catalytic subunit, nucleotidyltransferase domain superfamily / mRNA-capping enzyme catalytic subunit, RNA triphosphatase domain superfamily / : / : / mRNA capping enzyme catalytic subunit, GTase, NTPase domain / mRNA-capping enzyme catalytic subunit, GTase, OB fold / Poxvirus mRNA capping enzyme, small subunit / Poxvirus mRNA capping enzyme, small subunit superfamily / Poxvirus mRNA capping enzyme, small subunit / mRNA capping enzyme, large subunit, ATPase/guanylyltransferase, virus / mRNA capping enzyme catalytic subunit, RNA triphosphatase domain / DNA-directed RNA polymerase, 18kDa subunit, poxviral / DNA-directed RNA polymerase, 35kDa subunit, poxviral / RNA polymerase, 22kDa subunit, poxviral / DNA-directed RNA polymerase, 19kDa subunit, poxviral / DNA-directed RNA polymerase, 7kDa polypeptide, chordopoxviral / RNA polymerase, 30kDa subunit, chordopox-type / RNA polymerase, 132kDa subunit, poxvirus-type / RNA polymerase, 30kDa subunit, chordopox-type, N-terminal / Poxvirus DNA-directed RNA polymerase, 18 kD subunit / Poxvirus DNA-directed RNA polymerase, 35 kD subunit / Poxvirus RNA polymerase 22 kDa subunit / Poxvirus DNA-directed RNA polymerase 19 kDa subunit / Chordopoxvirus DNA-directed RNA polymerase 7 kDa polypeptide (RPO7) / Poxvirus DNA dependent RNA polymerase 30kDa subunit / Poxvirus DNA dependent RNA polymerase / mRNA (guanine-N(7))-methyltransferase domain / mRNA cap guanine-N7 methyltransferase / mRNA (guanine-N(7))-methyltransferase domain / mRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.56) domain profile. / Zinc finger TFIIS-type signature. / RNA polymerase Rpb2, domain 5 / RNA polymerase Rpb2, domain 5 / Zinc finger, TFIIS-type / Transcription factor S-II (TFIIS) / Zinc finger TFIIS-type profile. / C2C2 Zinc finger / RNA polymerase Rpb1, domain 3 superfamily / RNA polymerase Rpb1, clamp domain superfamily / DNA-directed RNA polymerase, subunit beta-prime / 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, 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 / 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 / S-adenosyl-L-methionine-dependent methyltransferase superfamily 類似検索 - ドメイン・相同性 DNA-directed RNA polymerase 30 kDa polypeptide / DNA-directed RNA polymerase 7 kDa subunit / DNA-directed RNA polymerase subunit / GTP--RNA guanylyltransferase / DNA-directed RNA polymerase 18 kDa subunit / Virus termination factor small subunit / DNA-directed RNA polymerase 19 kDa subunit / ポリメラーゼ / DNA-directed RNA polymerase 35 kDa subunit / DNA-directed RNA polymerase 30 kDa polypeptide ... DNA-directed RNA polymerase 30 kDa polypeptide / DNA-directed RNA polymerase 7 kDa subunit / DNA-directed RNA polymerase subunit / GTP--RNA guanylyltransferase / DNA-directed RNA polymerase 18 kDa subunit / Virus termination factor small subunit / DNA-directed RNA polymerase 19 kDa subunit / ポリメラーゼ / DNA-directed RNA polymerase 35 kDa subunit / DNA-directed RNA polymerase 30 kDa polypeptide / DNA-directed RNA polymerase 147 kDa polypeptide / DNA-directed RNA polymerase 35 kDa subunit / mRNA-capping enzyme catalytic subunit / mRNA-capping enzyme regulatory subunit OPG124 / DNA-directed RNA polymerase 7 kDa subunit / DNA-directed RNA polymerase 22 kDa subunit / DNA-directed RNA polymerase 147 kDa polypeptide / DNA-directed RNA polymerase 133 kDa polypeptide / DNA-directed RNA polymerase 19 kDa subunit / DNA-directed RNA polymerase 18 kDa subunit 類似検索 - 構成要素生物種 Vaccinia virus (ワクチニアウイルス)手法 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度 : 3.1 Å 詳細 データ登録者Hillen HS / Bartuli J / Grimm C / Dienemann C / Bedenk K / Szalar A / Fischer U / Cramer P 資金援助 ドイツ, 7件 詳細 詳細を隠すOrganization Grant number 国 German Research Foundation SFB860 ドイツ German Federal Ministry for Education and Research EXC 2067/1- 390729940 ドイツ German Research Foundation SPP1935 ドイツ Volkswagen Foundation ドイツ European Research Council TRANSREGULON ドイツ German Research Foundation Fi 573 18-1 ドイツ German Research Foundation Fi 573 7-2 ドイツ
引用ジャーナル : Cell / 年 : 2019タイトル : Structural Basis of Poxvirus Transcription: Transcribing and Capping Vaccinia Complexes.著者 : Hauke S Hillen / Julia Bartuli / Clemens Grimm / Christian Dienemann / Kristina Bedenk / Aladar A Szalay / Utz Fischer / Patrick Cramer / 要旨 : Poxviruses use virus-encoded multisubunit RNA polymerases (vRNAPs) and RNA-processing factors to generate mG-capped mRNAs in the host cytoplasm. In the accompanying paper, we report structures of ... Poxviruses use virus-encoded multisubunit RNA polymerases (vRNAPs) and RNA-processing factors to generate mG-capped mRNAs in the host cytoplasm. In the accompanying paper, we report structures of core and complete vRNAP complexes of the prototypic Vaccinia poxvirus (Grimm et al., 2019; in this issue of Cell). Here, we present the cryo-electron microscopy (cryo-EM) structures of Vaccinia vRNAP in the form of a transcribing elongation complex and in the form of a co-transcriptional capping complex that contains the viral capping enzyme (CE). The trifunctional CE forms two mobile modules that bind the polymerase surface around the RNA exit tunnel. RNA extends from the vRNAP active site through this tunnel and into the active site of the CE triphosphatase. Structural comparisons suggest that growing RNA triggers large-scale rearrangements on the surface of the transcription machinery during the transition from transcription initiation to RNA capping and elongation. Our structures unravel the basis for synthesis and co-transcriptional modification of poxvirus RNA. 履歴 登録 2019年4月23日 - ヘッダ(付随情報) 公開 2019年12月18日 - マップ公開 2019年12月18日 - 更新 2020年12月2日 - 現状 2020年12月2日 処理サイト : PDBe / 状態 : 公開
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