- EMDB-15364: Cryo-EM structure of the SEA complex (consensus map) -
+
データを開く
IDまたはキーワード:
読み込み中...
-
基本情報
登録情報
データベース: EMDB / ID: EMD-15364
タイトル
Cryo-EM structure of the SEA complex (consensus map)
マップデータ
DeepEMhancer sharpened map (wide mask)
試料
複合体: Seh1-associated complex (SEAC)
タンパク質・ペプチド: Maintenance of telomere capping protein 5
タンパク質・ペプチド: Nucleoporin SEH1
タンパク質・ペプチド: SEH-associated protein 4
タンパク質・ペプチド: Protein transport protein SEC13
タンパク質・ペプチド: Restriction of telomere capping protein 1
タンパク質・ペプチド: Nitrogen permease regulator 3
タンパク質・ペプチド: Vacuolar membrane-associated protein IML1
タンパク質・ペプチド: Nitrogen permease regulator 2
リガンド: ZINC ION
キーワード
GTPase activating protein / coatomer / TOR signaling / SIGNALING PROTEIN
機能・相同性
機能・相同性情報
urea transport / GATOR1 complex / negative regulation of small GTPase mediated signal transduction / pseudohyphal growth / GATOR2 complex / Seh1-associated complex / positive regulation of ER to Golgi vesicle-mediated transport / protein exit from endoplasmic reticulum / COPII-coated vesicle budding / proline transport ...urea transport / GATOR1 complex / negative regulation of small GTPase mediated signal transduction / pseudohyphal growth / GATOR2 complex / Seh1-associated complex / positive regulation of ER to Golgi vesicle-mediated transport / protein exit from endoplasmic reticulum / COPII-coated vesicle budding / proline transport / COPII-mediated vesicle transport / nuclear pore localization / regulation of TORC1 signaling / nuclear pore outer ring / COPII vesicle coat / positive regulation of protein exit from endoplasmic reticulum / TORC1 signaling / Transport of Mature mRNA derived from an Intron-Containing Transcript / Regulation of HSF1-mediated heat shock response / fungal-type vacuole / regulation of autophagosome assembly / SUMOylation of SUMOylation proteins / SUMOylation of RNA binding proteins / structural constituent of nuclear pore / SUMOylation of chromatin organization proteins / fungal-type vacuole membrane / negative regulation of TOR signaling / cellular response to nitrogen starvation / nucleocytoplasmic transport / vacuolar membrane / positive regulation of macroautophagy / positive regulation of TOR signaling / mRNA transport / nuclear pore / positive regulation of autophagy / signaling adaptor activity / ERAD pathway / negative regulation of TORC1 signaling / positive regulation of TORC1 signaling / cellular response to amino acid starvation / GTPase activator activity / meiotic cell cycle / cell periphery / protein import into nucleus / protein transport / nuclear envelope / cellular response to oxidative stress / nuclear membrane / intracellular signal transduction / response to xenobiotic stimulus / endoplasmic reticulum membrane / positive regulation of DNA-templated transcription / structural molecule activity / endoplasmic reticulum / metal ion binding / cytosol / cytoplasm 類似検索 - 分子機能
WD repeat protein mio, zinc-ribbon like domain / GATOR complex protein WDR24 / MIOS/Sea4 / : / Zinc-ribbon like family / MIOS, alpha-solenoid / : / : / RING/Ubox like zinc-binding domain / Nitrogen permease regulator 3 ...WD repeat protein mio, zinc-ribbon like domain / GATOR complex protein WDR24 / MIOS/Sea4 / : / Zinc-ribbon like family / MIOS, alpha-solenoid / : / : / RING/Ubox like zinc-binding domain / Nitrogen permease regulator 3 / Nitrogen permease regulator 2 / Vacuolar membrane-associated protein Iml1 / DEPDC5 protein, C-terminal / : / Nitrogen Permease regulator of amino acid transport activity 3 / Nitrogen permease regulator 2 / Vacuolar membrane-associated protein Iml1, N-terminal domain / DEPDC5 protein C-terminal region / RWD domain / RWD domain profile. / RWD / RWD domain / Sec13/Seh1 family / Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP) / DEP domain profile. / Domain found in Dishevelled, Egl-10, and Pleckstrin / DEP domain / Zinc finger RING-type profile. / Zinc finger, RING-type / Zinc finger, RING/FYVE/PHD-type / Winged helix DNA-binding domain superfamily / 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 / Winged helix-like DNA-binding domain superfamily / WD40/YVTN repeat-like-containing domain superfamily 類似検索 - ドメイン・相同性
SEH-associated protein 4 / Nitrogen permease regulator 3 / Nitrogen permease regulator 2 / Vacuolar membrane-associated protein IML1 / Nucleoporin SEH1 / Maintenance of telomere capping protein 5 / Protein transport protein SEC13 / Restriction of telomere capping protein 1 類似検索 - 構成要素
ジャーナル: Nature / 年: 2022 タイトル: Cryo-EM structure of the SEA complex. 著者: Lucas Tafur / Kerstin Hinterndorfer / Caroline Gabus / Chiara Lamanna / Ariane Bergmann / Yashar Sadian / Farzad Hamdi / Fotis L Kyrilis / Panagiotis L Kastritis / Robbie Loewith / 要旨: The SEA complex (SEAC) is a growth regulator that acts as a GTPase-activating protein (GAP) towards Gtr1, a Rag GTPase that relays nutrient status to the Target of Rapamycin Complex 1 (TORC1) in ...The SEA complex (SEAC) is a growth regulator that acts as a GTPase-activating protein (GAP) towards Gtr1, a Rag GTPase that relays nutrient status to the Target of Rapamycin Complex 1 (TORC1) in yeast. Functionally, the SEAC has been divided into two subcomplexes: SEACIT, which has GAP activity and inhibits TORC1, and SEACAT, which regulates SEACIT. This system is conserved in mammals: the GATOR complex, consisting of GATOR1 (SEACIT) and GATOR2 (SEACAT), transmits amino acid and glucose signals to mTORC1. Despite its importance, the structure of SEAC/GATOR, and thus molecular understanding of its function, is lacking. Here, we solve the cryo-EM structure of the native eight-subunit SEAC. The SEAC has a modular structure in which a COPII-like cage corresponding to SEACAT binds two flexible wings, which correspond to SEACIT. The wings are tethered to the core via Sea3, which forms part of both modules. The GAP mechanism of GATOR1 is conserved in SEACIT, and GAP activity is unaffected by SEACAT in vitro. In vivo, the wings are essential for recruitment of the SEAC to the vacuole, primarily via the EGO complex. Our results indicate that rather than being a direct inhibitor of SEACIT, SEACAT acts as a scaffold for the binding of TORC1 regulators.
chain_id: A, source_name: PDB, initial_model_type: experimental model
詳細
AlphaFold predictions were used as starting models for Sea1, Sea2, Sea3, Sea4, Npr2 and Npr3. Rigid body fit was performed in Chimera, and manual building in Coot.