登録情報 データベース : EMDB / ID : EMD-12799 構造の表示 ダウンロードとリンクタイトル SRP-SR at the distal site conformation マップデータSRP-SR complex from 3D focused refinement on ribosome signal subtracted images 詳細 試料複合体 : SRP-SR complex複合体 : SRP-SR complexRNA : x 1種タンパク質・ペプチド : x 4種複合体 : EM14S01-3B_G0054400.mRNA.1.CDS.1複合体 : Signal recognition particle receptor subunitリガンド : x 3種 詳細 キーワード SRP SRP receptor / co-translational protein targeting / endoplasmic reticulum / signal peptide / RNA BINDING 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
SRP-dependent cotranslational protein targeting to membrane / signal recognition particle receptor complex / SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition / endoplasmic reticulum signal peptide binding / signal recognition particle, endoplasmic reticulum targeting / granulocyte differentiation / signal recognition particle binding / protein localization to Golgi apparatus / protein targeting to ER / signal-recognition-particle GTPase ... SRP-dependent cotranslational protein targeting to membrane / signal recognition particle receptor complex / SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition / endoplasmic reticulum signal peptide binding / signal recognition particle, endoplasmic reticulum targeting / granulocyte differentiation / signal recognition particle binding / protein localization to Golgi apparatus / protein targeting to ER / signal-recognition-particle GTPase / SRP-dependent cotranslational protein targeting to membrane, translocation / Golgi to plasma membrane protein transport / 7S RNA binding / SRP-dependent cotranslational protein targeting to membrane / exocrine pancreas development / TPR domain binding / membrane => GO:0016020 / aminopeptidase activity / ribonucleoprotein complex binding / cytoplasmic microtubule / neutrophil chemotaxis / intracellular protein transport / GDP binding / ribosome binding / nuclear speck / serine-type endopeptidase activity / GTPase activity / endoplasmic reticulum membrane / GTP binding / nucleolus / endoplasmic reticulum / Golgi apparatus / ATP hydrolysis activity / nucleoplasm / nucleus / cytosol 類似検索 - 分子機能 Signal recognition particle receptor, alpha subunit, N-terminal / Signal recognition particle, alpha subunit, N-terminal / Signal recognition particle receptor, beta subunit / Signal recognition particle receptor beta subunit / Signal recognition particle, SRP72 subunit, RNA-binding / Signal recognition particle, SRP72 subunit / Putative TPR-like repeat / SRP72 RNA-binding domain / Putative TPR-like repeat / Signal recognition particle subunit SRP68 ... Signal recognition particle receptor, alpha subunit, N-terminal / Signal recognition particle, alpha subunit, N-terminal / Signal recognition particle receptor, beta subunit / Signal recognition particle receptor beta subunit / Signal recognition particle, SRP72 subunit, RNA-binding / Signal recognition particle, SRP72 subunit / Putative TPR-like repeat / SRP72 RNA-binding domain / Putative TPR-like repeat / Signal recognition particle subunit SRP68 / Signal recognition particle subunit SRP68, RNA-binding domain / SRP68, N-terminal domain superfamily / RNA-binding signal recognition particle 68 / Signal recognition particle, SRP54 subunit, eukaryotic / Signal recognition particle, SRP19 subunit / Signal recognition particle, subunit SRP19-like superfamily / SRP19 protein / SRP/SRP receptor, N-terminal / Signal recognition particle, SRP54 subunit / Signal recognition particle, SRP54 subunit, M-domain / Signal recognition particle, SRP54 subunit, M-domain superfamily / Signal peptide binding domain / SRP54-type proteins GTP-binding domain signature. / Signal recognition particle SRP54, helical bundle / Signal recognition particle SRP54, N-terminal domain superfamily / SRP54-type protein, helical bundle domain / SRP54-type protein, helical bundle domain / Signal recognition particle, SRP54 subunit, GTPase domain / SRP54-type protein, GTPase domain / SRP54-type protein, GTPase domain / Small GTPase superfamily, ARF type / Small GTPase Arf domain profile. / Prolyl endopeptidase family serine active site. / Peptidase S9, serine active site / Dipeptidylpeptidase IV, N-terminal domain / Dipeptidyl peptidase IV (DPP IV) N-terminal region / Longin-like domain superfamily / Peptidase S9, prolyl oligopeptidase, catalytic domain / Prolyl oligopeptidase family / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Tetratricopeptide-like helical domain superfamily / Alpha/Beta hydrolase fold / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase 類似検索 - ドメイン・相同性 SRP receptor subunit alpha / EM14S01-3B_G0054400.mRNA.1.CDS.1 / Signal recognition particle receptor subunit beta / Signal recognition particle 19 kDa protein / Signal recognition particle subunit SRP72 / Signal recognition particle subunit SRP54 / Signal recognition particle subunit SRP68 類似検索 - 構成要素生物種 Canis lupus familiaris (イヌ) / Saccharomyces cerevisiae (パン酵母) / Oryctolagus cuniculus (ウサギ)手法 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度 : 3.9 Å 詳細 データ登録者Jomaa A / Ban N 資金援助 スイス, 1件 詳細 詳細を隠すOrganization Grant number 国 Swiss National Science Foundation スイス
引用ジャーナル : Cell Rep / 年 : 2021タイトル : Molecular mechanism of cargo recognition and handover by the mammalian signal recognition particle.
著者 :
Ahmad Jomaa / Simon Eitzinger / Zikun Zhu / Sowmya Chandrasekar / Kan Kobayashi / Shu-Ou Shan / Nenad Ban / 要旨 :
Co-translational protein targeting to membranes by the signal recognition particle (SRP) is a universally conserved pathway from bacteria to humans. In mammals, SRP and its receptor (SR) have many ... Co-translational protein targeting to membranes by the signal recognition particle (SRP) is a universally conserved pathway from bacteria to humans. In mammals, SRP and its receptor (SR) have many additional RNA features and protein components compared to the bacterial system, which were recently shown to play regulatory roles. Due to its complexity, the mammalian SRP targeting process is mechanistically not well understood. In particular, it is not clear how SRP recognizes translating ribosomes with exposed signal sequences and how the GTPase activity of SRP and SR is regulated. Here, we present electron cryo-microscopy structures of SRP and SRP·SR in complex with the translating ribosome. The structures reveal the specific molecular interactions between SRP and the emerging signal sequence and the elements that regulate GTPase activity of SRP·SR. Our results suggest the molecular mechanism of how eukaryote-specific elements regulate the early and late stages of SRP-dependent protein targeting. 残り1件を表示 表示を減らす履歴 登録 2021年4月23日 - ヘッダ(付随情報) 公開 2021年7月21日 - マップ公開 2021年7月21日 - 更新 2024年7月10日 - 現状 2024年7月10日 処理サイト : PDBe / 状態 : 公開
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