- EMDB-23003: Cryo-EM structure of Saccharomyces cerevisiae ER membrane protein... -
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基本情報
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データベース: EMDB / ID: EMD-23003
タイトル
Cryo-EM structure of Saccharomyces cerevisiae ER membrane protein complex bound to Fab-DH4 in lipid nanodiscs
マップデータ
sharpened EM map of yEMC in lipid nanodiscs
試料
複合体: S. cerevisiae endoplasmic reticulum membrane protein complex (EMC) bound to Fab DH4 in yeast total extract lipid nanodiscs
複合体: endoplasmic reticulum membrane protein complex
タンパク質・ペプチド: x 9種
複合体: Fab DH4
タンパク質・ペプチド: x 2種
リガンド: x 2種
機能・相同性
機能・相同性情報
EMC complex / protein insertion into ER membrane by stop-transfer membrane-anchor sequence / protein folding in endoplasmic reticulum / phospholipid transport / autophagosome assembly / phospholipid metabolic process / endoplasmic reticulum to Golgi vesicle-mediated transport / protein transport / protein-folding chaperone binding / endoplasmic reticulum membrane ...EMC complex / protein insertion into ER membrane by stop-transfer membrane-anchor sequence / protein folding in endoplasmic reticulum / phospholipid transport / autophagosome assembly / phospholipid metabolic process / endoplasmic reticulum to Golgi vesicle-mediated transport / protein transport / protein-folding chaperone binding / endoplasmic reticulum membrane / endoplasmic reticulum / membrane / nucleus 類似検索 - 分子機能
Protein Sop4 / Suppressor of PMA 1-7 protein / TMEM85/ER membrane protein complex subunit 4 / Protein of unknown function (DUF1077) / ER membrane protein complex subunit 6 / ER membrane protein complex subunit 3 / ER membrane protein complex subunit 1, C-terminal / Membrane magnesium transporter / ER membrane protein complex subunit 1 / ER membrane protein complex subunit 6-like ...Protein Sop4 / Suppressor of PMA 1-7 protein / TMEM85/ER membrane protein complex subunit 4 / Protein of unknown function (DUF1077) / ER membrane protein complex subunit 6 / ER membrane protein complex subunit 3 / ER membrane protein complex subunit 1, C-terminal / Membrane magnesium transporter / ER membrane protein complex subunit 1 / ER membrane protein complex subunit 6-like / EMC6 / ER membrane protein complex subunit 1, C-terminal / Membrane magnesium transporter / ER membrane protein complex subunit 10 / ER membrane protein complex subunit 2-like / Integral membrane protein EMC3/TMCO1-like / Integral membrane protein EMC3/TMCO1-like / Integral membrane protein DUF106 / TPR repeat profile. / Tetratricopeptide repeat / Tetratricopeptide-like helical domain superfamily 類似検索 - ドメイン・相同性
ER membrane protein complex subunit 1 / ER membrane protein complex subunit 3 / Protein SOP4 / ER membrane protein complex subunit 5 / ER membrane protein complex subunit 2 / ER membrane protein complex subunit 4 / Endoplasmic reticulum membrane protein complex subunit 10 / ER membrane protein complex subunit 6 類似検索 - 構成要素
National Institutes of Health/Office of the Director
1DP2OD017690-01
米国
引用
ジャーナル: Elife / 年: 2020 タイトル: Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients. 著者: Lakshmi E Miller-Vedam / Bastian Bräuning / Katerina D Popova / Nicole T Schirle Oakdale / Jessica L Bonnar / Jesuraj R Prabu / Elizabeth A Boydston / Natalia Sevillano / Matthew J Shurtleff ...著者: Lakshmi E Miller-Vedam / Bastian Bräuning / Katerina D Popova / Nicole T Schirle Oakdale / Jessica L Bonnar / Jesuraj R Prabu / Elizabeth A Boydston / Natalia Sevillano / Matthew J Shurtleff / Robert M Stroud / Charles S Craik / Brenda A Schulman / Adam Frost / Jonathan S Weissman / 要旨: Membrane protein biogenesis in the endoplasmic reticulum (ER) is complex and failure-prone. The ER membrane protein complex (EMC), comprising eight conserved subunits, has emerged as a central player ...Membrane protein biogenesis in the endoplasmic reticulum (ER) is complex and failure-prone. The ER membrane protein complex (EMC), comprising eight conserved subunits, has emerged as a central player in this process. Yet, we have limited understanding of how EMC enables insertion and integrity of diverse clients, from tail-anchored to polytopic transmembrane proteins. Here, yeast and human EMC cryo-EM structures reveal conserved intricate assemblies and human-specific features associated with pathologies. Structure-based functional studies distinguish between two separable EMC activities, as an insertase regulating tail-anchored protein levels and a broader role in polytopic membrane protein biogenesis. These depend on mechanistically coupled yet spatially distinct regions including two lipid-accessible membrane cavities which confer client-specific regulation, and a non-insertase EMC function mediated by the EMC lumenal domain. Our studies illuminate the structural and mechanistic basis of EMC's multifunctionality and point to its role in differentially regulating the biogenesis of distinct client protein classes.
超分子 #1: S. cerevisiae endoplasmic reticulum membrane protein complex (EMC...
超分子
名称: S. cerevisiae endoplasmic reticulum membrane protein complex (EMC) bound to Fab DH4 in yeast total extract lipid nanodiscs タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: #1-#11
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超分子 #2: endoplasmic reticulum membrane protein complex