登録情報 データベース : EMDB / ID : EMD-4300 構造の表示 ダウンロードとリンクタイトル Structure of a prehandover mammalian ribosomal SRP and SRP receptor targeting complex マップデータ 詳細 試料複合体 : Translating ribosome bound to SRP and SRP receptor複合体 : RibosomeRNA : x 4種タンパク質・ペプチド : x 45種複合体 : SRPRNA : x 1種タンパク質・ペプチド : x 6種複合体 : SRP receptor複合体 : Signal sequenceリガンド : x 4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
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 / negative regulation of translational elongation ... 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 / negative regulation of translational elongation / 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 / ribonucleoprotein complex binding / cytoplasmic microtubule / neutrophil chemotaxis / intracellular protein transport / GDP binding / ribosome binding / nuclear speck / 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, SRP9 subunit ... 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, SRP9 subunit / SRP9 domain / Signal recognition particle SRP9 / Signal recognition particle 9 kDa protein (SRP9) / Signal recognition particle, SRP14 subunit / Signal recognition particle, SRP9/SRP14 subunit / Signal recognition particle 14kD protein / 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 family profile. / Longin-like domain superfamily / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Tetratricopeptide-like helical domain superfamily / 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 Signal recognition particle receptor subunit beta / SRP receptor subunit alpha / Signal recognition particle 19 kDa protein / Signal recognition particle 14 kDa protein / Signal recognition particle 9 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 Oryctolagus cuniculus (ウサギ) / Canis lupus familiaris (イヌ) / Saccharomyces cerevisiae (パン酵母) / Rabbit (ウサギ) / Dog (イヌ)手法 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度 : 3.7 Å 詳細 データ登録者Kobayashi K / Jomaa A / Ban N 引用ジャーナル : Science / 年 : 2018タイトル : Structure of a prehandover mammalian ribosomal SRP·SRP receptor targeting complex.著者 : Kan Kobayashi / Ahmad Jomaa / Jae Ho Lee / Sowmya Chandrasekar / Daniel Boehringer / Shu-Ou Shan / Nenad Ban / 要旨 : Signal recognition particle (SRP) targets proteins to the endoplasmic reticulum (ER). SRP recognizes the ribosome synthesizing a signal sequence and delivers it to the SRP receptor (SR) on the ER ... Signal recognition particle (SRP) targets proteins to the endoplasmic reticulum (ER). SRP recognizes the ribosome synthesizing a signal sequence and delivers it to the SRP receptor (SR) on the ER membrane followed by the transfer of the signal sequence to the translocon. Here, we present the cryo-electron microscopy structure of the mammalian translating ribosome in complex with SRP and SR in a conformation preceding signal sequence handover. The structure visualizes all eukaryotic-specific SRP and SR proteins and reveals their roles in stabilizing this conformation by forming a large protein assembly at the distal site of SRP RNA. We provide biochemical evidence that the guanosine triphosphate hydrolysis of SRP·SR is delayed at this stage, possibly to provide a time window for signal sequence handover to the translocon. 履歴 登録 2018年2月16日 - ヘッダ(付随情報) 公開 2018年3月28日 - マップ公開 2018年3月28日 - 更新 2018年5月2日 - 現状 2018年5月2日 処理サイト : PDBe / 状態 : 公開
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