登録情報 データベース : EMDB / ID : EMD-32060 構造の表示 ダウンロードとリンクタイトル Cryo-EM structure of Xenopus laevis nuclear pore complex cytoplasmic ring subunit core region マップデータ 詳細 試料複合体 : nuclear pore complex cytoplasmic ring 詳細 キーワード cytoplasmic ring / cryo-EM / nuclear pore complex / Xenopus laevis / 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
macromolecule localization / GATOR2 complex / nephron development / nuclear pore organization / nuclear pore outer ring / nuclear pore complex assembly / attachment of mitotic spindle microtubules to kinetochore / structural constituent of nuclear pore / nucleocytoplasmic transport / mitotic metaphase chromosome alignment ... macromolecule localization / GATOR2 complex / nephron development / nuclear pore organization / nuclear pore outer ring / nuclear pore complex assembly / attachment of mitotic spindle microtubules to kinetochore / structural constituent of nuclear pore / nucleocytoplasmic transport / mitotic metaphase chromosome alignment / ribosomal large subunit export from nucleus / intracellular transport / mRNA transport / cellular response to nutrient levels / nuclear pore / ribosomal small subunit export from nucleus / positive regulation of TORC1 signaling / nuclear periphery / kinetochore / protein transport / nuclear membrane / lysosomal membrane / cell division / structural molecule activity / metal ion binding / cytosol 類似検索 - 分子機能 Nucleoporin Nup88 / Nuclear pore component / Nucleoporin NUP88/NUP82 / Nucleoporin Nup120/160 / Nucleoporin Nup37 / Nucleoporin, NSP1-like, C-terminal / Nucleoporin NSP1/NUP62 / Nsp1-like C-terminal region / Nucleoporin Nup85-like / Nucleoporin Nup120/160 ... Nucleoporin Nup88 / Nuclear pore component / Nucleoporin NUP88/NUP82 / Nucleoporin Nup120/160 / Nucleoporin Nup37 / Nucleoporin, NSP1-like, C-terminal / Nucleoporin NSP1/NUP62 / Nsp1-like C-terminal region / Nucleoporin Nup85-like / Nucleoporin Nup120/160 / Nup85 Nucleoporin / Nuclear pore protein 84/107 / Nuclear pore protein 84 / 107 / Nuclear pore complex protein Nup133-like / Nup98, Gle2-binding sequence / Nucleoporin Nup186/Nup192/Nup205 / Nuclear pore complex protein / Nuclear pore complex scaffold, nucleoporins 186/192/205 / Nucleoporin interacting component Nup93/Nic96 / Nup358/RanBP2 E3 ligase domain / Nup93/Nic96 / Nup358/RanBP2 E3 ligase domain / Nucleoporin FG repeat / Nucleoporin FG repeat region / Nucleoporin, Nup133/Nup155-like, N-terminal / Nup133 N terminal like / Sec13/Seh1 family / Nuclear pore complex protein NUP96, C-terminal domain / Nuclear protein 96 / Nuclear pore complex protein Nup98-Nup96-like, autopeptidase S59 domain / Nuclear pore complex protein Nup98-Nup96-like, autopeptidase S59 domain superfamily / Nucleoporin peptidase S59-like / Nucleoporin autopeptidase / NUP C-terminal domain profile. / Ran binding domain / Ran binding protein RanBP1-like / RanBP1 domain / Ran binding domain type 1 profile. / Ran-binding domain / Zinc finger domain / Zn-finger in Ran binding protein and others / Zinc finger RanBP2 type profile. / Zinc finger RanBP2-type signature. / Zinc finger, RanBP2-type superfamily / Zinc finger, RanBP2-type / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Tetratricopeptide-like helical domain superfamily / PH-like domain superfamily / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily 類似検索 - ドメイン・相同性 Nuclear pore complex protein Nup98-Nup96 / Nuclear pore complex protein Nup133 / RANBP2-like and GRIP domain-containing protein 3 isoform X2 / Nucleoporin 160kDa / Nuclear pore complex protein / MGC154553 protein / Nucleoporin SEH1-A / Nucleoporin 88kDa L homeolog / MGC83295 protein / MGC83926 protein ... Nuclear pore complex protein Nup98-Nup96 / Nuclear pore complex protein Nup133 / RANBP2-like and GRIP domain-containing protein 3 isoform X2 / Nucleoporin 160kDa / Nuclear pore complex protein / MGC154553 protein / Nucleoporin SEH1-A / Nucleoporin 88kDa L homeolog / MGC83295 protein / MGC83926 protein / Nuclear pore complex protein Nup85 / Nuclear pore complex protein Nup93 / Protein SEC13 homolog / IL4I1 protein / Nucleoporin 214 L homeolog 類似検索 - 構成要素生物種 Xenopus laevis (アフリカツメガエル)手法 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度 : 7.9 Å 詳細 データ登録者Tai L / Zhu Y / Sun F 資金援助 1件 詳細 詳細を隠すOrganization Grant number 国 Not funded
引用ジャーナル : Protein Cell / 年 : 2022タイトル : 8 Å structure of the outer rings of the Xenopus laevis nuclear pore complex obtained by cryo-EM and AI.著者 : Linhua Tai / Yun Zhu / He Ren / Xiaojun Huang / Chuanmao Zhang / Fei Sun / 要旨 : The nuclear pore complex (NPC), one of the largest protein complexes in eukaryotes, serves as a physical gate to regulate nucleocytoplasmic transport. Here, we determined the 8 Å resolution cryo- ... The nuclear pore complex (NPC), one of the largest protein complexes in eukaryotes, serves as a physical gate to regulate nucleocytoplasmic transport. Here, we determined the 8 Å resolution cryo-electron microscopic (cryo-EM) structure of the outer rings containing nuclear ring (NR) and cytoplasmic ring (CR) from the Xenopus laevis NPC, with local resolutions reaching 4.9 Å. With the aid of AlphaFold2, we managed to build a pseudoatomic model of the outer rings, including the Y complexes and flanking components. In this most comprehensive and accurate model of outer rings to date, the almost complete Y complex structure exhibits much tighter interaction in the hub region. In addition to two copies of Y complexes, each asymmetric subunit in CR contains five copies of Nup358, two copies of the Nup214 complex, two copies of Nup205 and one copy of newly identified Nup93, while that in NR contains one copy of Nup205, one copy of ELYS and one copy of Nup93. These in-depth structural features represent a great advance in understanding the assembly of NPCs. 履歴 登録 2021年10月14日 - ヘッダ(付随情報) 公開 2022年2月2日 - マップ公開 2022年2月2日 - 更新 2023年12月13日 - 現状 2023年12月13日 処理サイト : PDBj / 状態 : 公開
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