登録情報 データベース : EMDB / ID : EMD-13793 ダウンロードとリンクタイトル Human 17S U2 snRNP 5' domain core マップデータ 詳細 試料複合体 : 17S U2 snRNP複合体 : 17S U2 snRNPタンパク質・ペプチド : x 7種RNA : x 1種複合体 : HIV Tat-specific factor 1リガンド : x 2種 詳細 キーワード snRNP / Spliceosome / U2 snRNP / Splicing / NUCLEAR PROTEIN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
U11/U12 snRNP / B-WICH complex / splicing factor binding / chromatin-protein adaptor activity / U12-type spliceosomal complex / poly-ADP-D-ribose modification-dependent protein binding / protein localization to site of double-strand break / RNA splicing, via transesterification reactions / U2-type precatalytic spliceosome / U2-type spliceosomal complex ... U11/U12 snRNP / B-WICH complex / splicing factor binding / chromatin-protein adaptor activity / U12-type spliceosomal complex / poly-ADP-D-ribose modification-dependent protein binding / protein localization to site of double-strand break / RNA splicing, via transesterification reactions / U2-type precatalytic spliceosome / U2-type spliceosomal complex / U2-type prespliceosome assembly / SAGA complex / U2 snRNP / U2-type prespliceosome / positive regulation of transcription by RNA polymerase III / precatalytic spliceosome / positive regulation of transcription by RNA polymerase I / spliceosomal complex assembly / regulation of RNA splicing / mRNA Splicing - Minor Pathway / mRNA 3'-splice site recognition / U2 snRNA binding / regulation of DNA repair / Cajal body / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / RNA splicing / stem cell differentiation / spliceosomal complex / double-strand break repair via homologous recombination / negative regulation of protein catabolic process / mRNA splicing, via spliceosome / B-WICH complex positively regulates rRNA expression / nuclear matrix / fibrillar center / mRNA processing / site of double-strand break / RNA helicase activity / nuclear speck / RNA helicase / chromatin remodeling / mRNA binding / protein-containing complex binding / positive regulation of DNA-templated transcription / nucleolus / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / RNA binding / zinc ion binding / nucleoplasm / ATP binding / nucleus 類似検索 - 分子機能 TatSF1-like, RNA recognition motif 1 / TatSF1-like / : / KH-domain / Splicing factor SF3a60 binding domain / Splicing factor SF3a60 binding domain / : / Replication stress response SDE2 C-terminal / Splicing factor SF3a60 /Prp9 subunit, C-terminal / SF3A3 domain ... TatSF1-like, RNA recognition motif 1 / TatSF1-like / : / KH-domain / Splicing factor SF3a60 binding domain / Splicing factor SF3a60 binding domain / : / Replication stress response SDE2 C-terminal / Splicing factor SF3a60 /Prp9 subunit, C-terminal / SF3A3 domain / SF3a60/Prp9 C-terminal / Pre-mRNA-splicing factor SF3A3, of SF3a complex, Prp9 / Splicing factor 3B, subunit 5 / Splicing factor 3B subunit 1 / : / Splicing factor 3B subunit 1 / : / Domain of unknown function DUF382 / Domain of unknown function (DUF382) / PHF5-like / PHF5-like protein / PSP, proline-rich / PSP / proline-rich domain in spliceosome associated proteins / Splicing factor 3B subunit 5/RDS3 complex subunit 10 / Splicing factor 3B subunit 10 (SF3b10) / Splicing factor 3B subunit 1-like / Matrin/U1-C, C2H2-type zinc finger / Zinc finger matrin-type profile. / : / PPP2R1A-like HEAT repeat / SAP motif profile. / SAP domain / Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation / SAP domain / DEAD-box subfamily ATP-dependent helicases signature. / RSE1/DDB1/CPSF1 second beta-propeller / ATP-dependent RNA helicase DEAD-box, conserved site / Cleavage/polyadenylation specificity factor, A subunit, C-terminal / Cleavage/polyadenylation specificity factor, A subunit, N-terminal / : / CPSF A subunit region / RSE1/DDB1/CPSF1 first beta-propeller / RNA helicase, DEAD-box type, Q motif / DEAD-box RNA helicase Q motif profile. / DEAD/DEAH box helicase domain / DEAD/DEAH box helicase / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Helicase conserved C-terminal domain / Armadillo-like helical / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / Armadillo-type fold / Nucleotide-binding alpha-beta plait domain superfamily / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / P-loop containing nucleoside triphosphate hydrolase 類似検索 - ドメイン・相同性 17S U2 SnRNP complex component HTATSF1 / Splicing factor 3B subunit 1 / Splicing factor 3A subunit 3 / Splicing factor 3B subunit 2 / Splicing factor 3B subunit 3 / Probable ATP-dependent RNA helicase DDX46 / PHD finger-like domain-containing protein 5A / Splicing factor 3B subunit 5 類似検索 - 構成要素生物種 Homo sapiens (ヒト)手法 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度 : 2.21 Å 詳細 データ登録者Tholen J / Galej WP 資金援助 European Union, 1件 詳細 詳細を隠すOrganization Grant number 国 European Research Council (ERC) 950278 European Union
引用ジャーナル : Science / 年 : 2022タイトル : Structural basis of branch site recognition by the human spliceosome.著者 : Jonas Tholen / Michal Razew / Felix Weis / Wojciech P Galej / 要旨 : Recognition of the intron branch site (BS) by the U2 small nuclear ribonucleoprotein (snRNP) is a critical event during spliceosome assembly. In mammals, BS sequences are poorly conserved, and ... Recognition of the intron branch site (BS) by the U2 small nuclear ribonucleoprotein (snRNP) is a critical event during spliceosome assembly. In mammals, BS sequences are poorly conserved, and unambiguous intron recognition cannot be achieved solely through a base-pairing mechanism. We isolated human 17 U2 snRNP and reconstituted in vitro its adenosine 5´-triphosphate (ATP)–dependent remodeling and binding to the pre–messenger RNA substrate. We determined a series of high-resolution (2.0 to 2.2 angstrom) structures providing snapshots of the BS selection process. The substrate-bound U2 snRNP shows that SF3B6 stabilizes the BS:U2 snRNA duplex, which could aid binding of introns with poor sequence complementarity. ATP-dependent remodeling uncoupled from substrate binding captures U2 snRNA in a conformation that competes with BS recognition, providing a selection mechanism based on branch helix stability. 履歴 登録 2021年10月28日 - ヘッダ(付随情報) 公開 2022年3月30日 - マップ公開 2022年3月30日 - 更新 2024年7月17日 - 現状 2024年7月17日 処理サイト : PDBe / 状態 : 公開
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