登録情報 データベース : EMDB / ID : EMD-41016 ダウンロードとリンクタイトル Structure of Bre1-nucleosome complex - state1 マップデータStructure of Bre1-nucleosome complex - state1 詳細 試料複合体 : Bre1-nucleosome complexタンパク質・ペプチド : Histone H3.2タンパク質・ペプチド : Histone H4タンパク質・ペプチド : Histone H2A type 1タンパク質・ペプチド : Histone H2BDNA : 601 DNA Strand 1DNA : 601 DNA Strand 2タンパク質・ペプチド : E3 ubiquitin-protein ligase BRE1 残り3件を表示 表示を減らすリガンド : ZINC ION 詳細 キーワード H2B ubiquitin E3 ligase / dimer / nucleosome acidic patch binding protein / DNA BINDING PROTEIN-Transferase-DNA complex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
HULC complex / meiotic DNA double-strand break formation / telomere maintenance via recombination / mitotic intra-S DNA damage checkpoint signaling / regulation of DNA-templated DNA replication initiation / DNA replication origin binding / subtelomeric heterochromatin formation / mitotic G1 DNA damage checkpoint signaling / double-strand break repair via homologous recombination / RING-type E3 ubiquitin transferase ... HULC complex / meiotic DNA double-strand break formation / telomere maintenance via recombination / mitotic intra-S DNA damage checkpoint signaling / regulation of DNA-templated DNA replication initiation / DNA replication origin binding / subtelomeric heterochromatin formation / mitotic G1 DNA damage checkpoint signaling / double-strand break repair via homologous recombination / RING-type E3 ubiquitin transferase / structural constituent of chromatin / ubiquitin protein ligase activity / nucleosome / nucleosome assembly / transcription by RNA polymerase II / chromosome, telomeric region / protein ubiquitination / protein heterodimerization activity / chromatin / DNA binding / nucleoplasm / identical protein binding / nucleus / metal ion binding 類似検索 - 分子機能 E3 ubiquitin ligase Bre1 / BRE1 E3 ubiquitin ligase / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / Ring finger / Zinc finger C2H2-type / Histone H2B signature. / Histone H2B / Histone H2B / Histone H2A conserved site ... E3 ubiquitin ligase Bre1 / BRE1 E3 ubiquitin ligase / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / Ring finger / Zinc finger C2H2-type / Histone H2B signature. / Histone H2B / Histone H2B / Histone H2A conserved site / Histone H2A signature. / Histone H2A, C-terminal domain / C-terminus of histone H2A / Histone H2A / Histone 2A / Histone H4, conserved site / Histone H4 signature. / Histone H4 / Histone H4 / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Zinc finger RING-type profile. / Histone H3/CENP-A / Zinc finger, RING-type / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold / Zinc finger, RING/FYVE/PHD-type 類似検索 - ドメイン・相同性 Histone H2B 1.1 / Histone H2A type 1 / Histone H4 / Histone H3.2 / E3 ubiquitin-protein ligase BRE1 類似検索 - 構成要素生物種 Saccharomyces cerevisiae (パン酵母) / Xenopus laevis (アフリカツメガエル) / Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (パン酵母) / synthetic construct (人工物) 手法 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度 : 3.47 Å 詳細 データ登録者Zhao F / Hicks CW / Wolberger C 資金援助 米国, 1件 詳細 詳細を隠すOrganization Grant number 国 National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) GM130393 米国
引用ジャーナル : Nat Struct Mol Biol / 年 : 2023タイトル : Mechanism of histone H2B monoubiquitination by Bre1.著者 : Fan Zhao / Chad W Hicks / Cynthia Wolberger / 要旨 : Monoubiquitination of histone H2B-K120/123 plays several roles in regulating transcription, DNA replication and the DNA damage response. The structure of a nucleosome in complex with the dimeric RING ... Monoubiquitination of histone H2B-K120/123 plays several roles in regulating transcription, DNA replication and the DNA damage response. The structure of a nucleosome in complex with the dimeric RING E3 ligase Bre1 reveals that one RING domain binds to the nucleosome acidic patch, where it can position the E2 ubiquitin conjugating enzyme Rad6, while the other RING domain contacts the DNA. Comparisons with H2A-specific E3 ligases suggest a general mechanism of tuning histone specificity via the non-E2-binding RING domain. 履歴 登録 2023年6月8日 - ヘッダ(付随情報) 公開 2023年10月18日 - マップ公開 2023年10月18日 - 更新 2023年11月22日 - 現状 2023年11月22日 処理サイト : RCSB / 状態 : 公開
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