- EMDB-39086: Structure of the SecA-SecY complex with the substrate HmBRI-3TM -
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基本情報
登録情報
データベース: EMDB / ID: EMD-39086
タイトル
Structure of the SecA-SecY complex with the substrate HmBRI-3TM
マップデータ
試料
複合体: SecA-SecY complex with the substrate HmBRI-3TM
タンパク質・ペプチド: Protein translocase subunit SecA
タンパク質・ペプチド: Protein translocase subunit SecY
タンパク質・ペプチド: Protein translocase subunit SecE
タンパク質・ペプチド: Nanobody
タンパク質・ペプチド: Bacteriorhodopsin-I
リガンド: MAGNESIUM ION
リガンド: BERYLLIUM TRIFLUORIDE ION
リガンド: ADENOSINE-5'-DIPHOSPHATE
キーワード
Protein translocation / Membrane protein insertion / Protein chaperone / PROTEIN TRANSPORT
機能・相同性
機能・相同性情報
protein-exporting ATPase activity / cell envelope Sec protein transport complex / protein-secreting ATPase / intracellular protein transmembrane transport / protein transport by the Sec complex / protein import / monoatomic ion channel activity / protein secretion / protein transmembrane transporter activity / photoreceptor activity ...protein-exporting ATPase activity / cell envelope Sec protein transport complex / protein-secreting ATPase / intracellular protein transmembrane transport / protein transport by the Sec complex / protein import / monoatomic ion channel activity / protein secretion / protein transmembrane transporter activity / photoreceptor activity / phototransduction / protein targeting / proton transmembrane transport / membrane raft / ATP binding / metal ion binding / membrane / plasma membrane / cytoplasm 類似検索 - 分子機能
SecE subunit of protein translocation complex, bacterial-like / SecE superfamily / SEC-C motif / SEC-C motif / Protein translocase subunit SecA / SecA DEAD-like, N-terminal / SecA Wing/Scaffold / SecA, preprotein cross-linking domain / SecA motor DEAD / SecA conserved site ...SecE subunit of protein translocation complex, bacterial-like / SecE superfamily / SEC-C motif / SEC-C motif / Protein translocase subunit SecA / SecA DEAD-like, N-terminal / SecA Wing/Scaffold / SecA, preprotein cross-linking domain / SecA motor DEAD / SecA conserved site / SecA, Wing/Scaffold superfamily / SecA, preprotein cross-linking domain superfamily / SecA, C-terminal helicase domain / SecA preprotein cross-linking domain / SecA Wing and Scaffold domain / SecA DEAD-like domain / SecA P-loop domain / SecA family signature. / SecA family profile. / SecA DEAD-like domain / SecA preprotein cross-linking domain / Protein translocase subunit SecY / Protein secE/sec61-gamma signature. / Protein secY signature 1. / Protein secY signature 2. / SecE/Sec61-gamma subunits of protein translocation complex / Protein translocase complex, SecE/Sec61-gamma subunit / SecY/SEC61-alpha family / SecY domain superfamily / SecY conserved site / SecY / Bacterial rhodopsins retinal binding site. / Bacterial rhodopsins signature 1. / Rhodopsin, retinal binding site / Bacteriorhodopsin-like protein / Archaeal/bacterial/fungal rhodopsins / Bacteriorhodopsin-like protein / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / P-loop containing nucleoside triphosphate hydrolase 類似検索 - ドメイン・相同性
Protein translocase subunit SecE / Protein translocase subunit SecY / Protein translocase subunit SecA / Bacteriorhodopsin-I 類似検索 - 構成要素
National Natural Science Foundation of China (NSFC)
31725007,31630087,31800625,21873006,31870835
中国
Other government
2018M631249,2019M650327
引用
ジャーナル: Cell / 年: 2025 タイトル: SecY translocon chaperones protein folding during membrane protein insertion. 著者: Xiaomin Ou / Chengying Ma / Dongjie Sun / Jinkun Xu / Yang Wang / Xiaofei Wu / Dali Wang / Song Yang / Ning Gao / Chen Song / Long Li / 要旨: The Sec translocon is vital for guiding membrane protein insertion into lipid bilayers. The insertion and folding processes of membrane proteins are poorly understood. Here, we report cryo-electron ...The Sec translocon is vital for guiding membrane protein insertion into lipid bilayers. The insertion and folding processes of membrane proteins are poorly understood. Here, we report cryo-electron microscopy structures of multi-spanning membrane proteins inserting through the SecY channel, the Sec translocon in prokaryotes. The high-resolution structures illustrate how bulky amino acids pass the narrow channel restriction. Comparison of different translocation states reveals that the cytoplasmic and extracellular cavities of the channel create distinct environments for promoting the unfolding and folding of transmembrane segments (TMs), respectively. Released substrate TMs are either flexible or stabilized by an unexpected hydrophilic groove between TM3 and TM4 of SecY. Disruption of the groove causes global defects in the folding of the membrane proteome. These findings demonstrate that beyond its role as a passive protein-conducting channel, the SecY translocon actively serves as a chaperone, employing multiple mechanisms to promote membrane protein insertion and folding.