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- EMDB-63442: Cryo-EM structure of dual sensor bound GATOR2 complex -

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Basic information

Entry
Database: EMDB / ID: EMD-63442
TitleCryo-EM structure of dual sensor bound GATOR2 complex
Map data
Sample
  • Complex: dual sensor bound GATOR2 complex
    • Protein or peptide: GATOR2 complex protein MIOS
    • Protein or peptide: GATOR2 complex protein WDR24
    • Protein or peptide: GATOR2 complex protein WDR59
    • Protein or peptide: Isoform B of Nucleoporin SEH1
    • Protein or peptide: Isoform 3 of Protein SEC13 homolog
    • Protein or peptide: Cytosolic arginine sensor for mTORC1 subunit 1
    • Protein or peptide: Sestrin-2
  • Ligand: ZINC ION
Keywordsamino acid sensor / STRUCTURAL PROTEIN
Function / homology
Function and homology information


oligodendrocyte progenitor proliferation / regulation of response to reactive oxygen species / sulfiredoxin activity / negative regulation of translation in response to endoplasmic reticulum stress / GATOR2 complex / L-leucine binding / cellular response to L-arginine / molecular sensor activity / Atg1/ULK1 kinase complex / Seh1-associated complex ...oligodendrocyte progenitor proliferation / regulation of response to reactive oxygen species / sulfiredoxin activity / negative regulation of translation in response to endoplasmic reticulum stress / GATOR2 complex / L-leucine binding / cellular response to L-arginine / molecular sensor activity / Atg1/ULK1 kinase complex / Seh1-associated complex / protein exit from endoplasmic reticulum / COPII-coated vesicle budding / TORC2 complex / regulation of TORC1 signaling / oxidoreductase activity, acting on peroxide as acceptor / central nervous system myelin formation / cellular response to leucine starvation / COPII-coated vesicle cargo loading / PH domain binding / nuclear pore outer ring / nuclear pore organization / COPII vesicle coat / mitochondrial DNA metabolic process / nucleotide-activated protein kinase complex / Nuclear Pore Complex (NPC) Disassembly / Transport of Ribonucleoproteins into the Host Nucleus / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) / Amino acids regulate mTORC1 / cellular response to L-leucine / protein K6-linked ubiquitination / attachment of mitotic spindle microtubules to kinetochore / Transport of the SLBP independent Mature mRNA / NS1 Mediated Effects on Host Pathways / Transport of the SLBP Dependant Mature mRNA / SUMOylation of SUMOylation proteins / protein-containing complex localization / Transport of Mature mRNA Derived from an Intronless Transcript / Rev-mediated nuclear export of HIV RNA / Nuclear import of Rev protein / SUMOylation of RNA binding proteins / NEP/NS2 Interacts with the Cellular Export Machinery / arginine binding / regulation of protein phosphorylation / Transport of Mature mRNA derived from an Intron-Containing Transcript / tRNA processing in the nucleus / Postmitotic nuclear pore complex (NPC) reformation / COPII-mediated vesicle transport / vacuolar membrane / positive regulation of lipophagy / GDP-dissociation inhibitor activity / nucleocytoplasmic transport / triglyceride homeostasis / regulation of gluconeogenesis / Viral Messenger RNA Synthesis / cellular oxidant detoxification / mitotic metaphase chromosome alignment / SUMOylation of ubiquitinylation proteins / fatty acid beta-oxidation / Vpr-mediated nuclear import of PICs / regulation of cAMP/PKA signal transduction / D-glucose import / oligodendrocyte differentiation / SUMOylation of DNA replication proteins / positive regulation of macroautophagy / Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases / positive regulation of TOR signaling / Regulation of HSF1-mediated heat shock response / mRNA transport / response to glucose / nuclear pore / SUMOylation of DNA damage response and repair proteins / cellular response to nutrient levels / cellular response to glucose starvation / negative regulation of TORC1 signaling / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / signaling adaptor activity / positive regulation of TORC1 signaling / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / MHC class II antigen presentation / reactive oxygen species metabolic process / cellular response to amino acid starvation / protein sequestering activity / Resolution of Sister Chromatid Cohesion / SUMOylation of chromatin organization proteins / HCMV Late Events / TP53 Regulates Metabolic Genes / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / cellular response to amino acid stimulus / DNA damage response, signal transduction by p53 class mediator / intracellular protein transport / peroxidase activity / Transcriptional regulation by small RNAs / ISG15 antiviral mechanism / RHO GTPases Activate Formins / ER to Golgi transport vesicle membrane / negative regulation of cell growth / response to insulin / RING-type E3 ubiquitin transferase
Similarity search - Function
Sestrin / WDR59, modified RING finger, H2 subclass (C3H3C2-type) / PA26 p53-induced protein (sestrin) / MIOS, WD40 repeat / CASTOR family / CASTOR1, N-terminal / : / Cytosolic arginine sensor for mTORC1 subunit 1 N-terminal domain / Cytosolic arginine sensor for mTORC1 subunit 1/2, ACT-like / WD repeat protein mio, zinc-ribbon like domain ...Sestrin / WDR59, modified RING finger, H2 subclass (C3H3C2-type) / PA26 p53-induced protein (sestrin) / MIOS, WD40 repeat / CASTOR family / CASTOR1, N-terminal / : / Cytosolic arginine sensor for mTORC1 subunit 1 N-terminal domain / Cytosolic arginine sensor for mTORC1 subunit 1/2, ACT-like / 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 / CASTOR, ACT domain / ACT domain / AhpD-like / RWD domain profile. / RWD / RWD domain / Sec13/Seh1 family / ACT-like domain / Ubiquitin-conjugating enzyme/RWD-like / WD domain, G-beta repeat / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
Protein SEC13 homolog / Sestrin-2 / GATOR2 complex protein WDR59 / Cytosolic arginine sensor for mTORC1 subunit 1 / Nucleoporin SEH1 / GATOR2 complex protein WDR24 / GATOR2 complex protein MIOS
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.41 Å
AuthorsSu M-Y
Funding support1 items
OrganizationGrant numberCountry
Other government
CitationJournal: Cell Rep / Year: 2025
Title: Cryo-EM structures of amino acid sensors bound to the human GATOR2 complex.
Authors: Ming-Yuan Su / Fei Teng / Shan Wang / Xinyi Mai / Huan Zeng / Juan Li / Xiaoxiao Song / Xi Wang / Goran Stjepanovic /
Abstract: Mammalian cells regulate growth by integrating environmental cues through the mammalian target of rapamycin complex 1 (mTORC1) signaling pathway. The human GATOR2 complex, comprising WDR59, WDR24, ...Mammalian cells regulate growth by integrating environmental cues through the mammalian target of rapamycin complex 1 (mTORC1) signaling pathway. The human GATOR2 complex, comprising WDR59, WDR24, Mios, Sec13, and Seh1l, is key to mTORC1 regulation. Under amino acid deprivation, GATOR2 is inhibited through interactions with cytosolic leucine sensor Sestrin2 and arginine sensor cytosolic arginine sensor for mTORC1 subunit 1 (CASTOR1). Amino acid abundance relieves this inhibition, allowing GATOR2 to antagonize the repressor GATOR1. Despite its importance, GATOR2's inhibition mechanisms were unclear. Here, we present cryo-electron microscopy (cryo-EM) structures of GATOR2 in three inhibitory states: CASTOR1 bound, Sestrin2 bound, and dual bound. CASTOR1 engages the Mios WD40 β-propellers, while Sestrin2 interacts with the WDR24-Seh1l subcomplex, inducing conformational movements. Hydrogen-deuterium exchange mass spectrometry (HDX-MS) reveals dynamic motions in apo-GATOR2 and its complexes with amino acid sensors, as well as the effects of amino acid supplementation. These findings unravel the interactions between GATOR2 and amino acid sensors, providing a perspective on the regulation of the mTORC1 pathway by nutrient-sensing machinery.
History
DepositionFeb 14, 2025-
Header (metadata) releaseAug 13, 2025-
Map releaseAug 13, 2025-
UpdateAug 13, 2025-
Current statusAug 13, 2025Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_63442.png

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Map

FileDownload / File: emd_63442.map.gz / Format: CCP4 / Size: 1.2 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
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AxesZ (Sec.)Y (Row.)X (Col.)
0.85 Å/pix.
x 680 pix.
= 578. Å		0.85 Å/pix.
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= 578. Å		0.85 Å/pix.
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= 578. Å

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Contour LevelBy AUTHOR: 0.103
Minimum - Maximum-0.18863668 - 0.93287796
Average (Standard dev.)-0.00012627913 (±0.026967948)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions680680680
Spacing680680680
CellA=B=C: 578.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Annotationdeepemhancer post process
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Sample components

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Entire : dual sensor bound GATOR2 complex

EntireName: dual sensor bound GATOR2 complex
Components
  • Complex: dual sensor bound GATOR2 complex
    • Protein or peptide: GATOR2 complex protein MIOS
    • Protein or peptide: GATOR2 complex protein WDR24
    • Protein or peptide: GATOR2 complex protein WDR59
    • Protein or peptide: Isoform B of Nucleoporin SEH1
    • Protein or peptide: Isoform 3 of Protein SEC13 homolog
    • Protein or peptide: Cytosolic arginine sensor for mTORC1 subunit 1
    • Protein or peptide: Sestrin-2
  • Ligand: ZINC ION

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Supramolecule #1: dual sensor bound GATOR2 complex

SupramoleculeName: dual sensor bound GATOR2 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#7
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: GATOR2 complex protein MIOS

MacromoleculeName: GATOR2 complex protein MIOS / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 98.700391 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSGTKPDILW APHHVDRFVV CDSELSLYHV ESTVNSELKA GSLRLSEDSA ATLLSINSDT PYMKCVAWYL NYDPECLLAV GQANGRVVL TSLGQDHNSK FKDLIGKEFV PKHARQCNTL AWNPLDSNWL AAGLDKHRAD FSVLIWDICS KYTPDIVPME K VKLSAGET ...String:
MSGTKPDILW APHHVDRFVV CDSELSLYHV ESTVNSELKA GSLRLSEDSA ATLLSINSDT PYMKCVAWYL NYDPECLLAV GQANGRVVL TSLGQDHNSK FKDLIGKEFV PKHARQCNTL AWNPLDSNWL AAGLDKHRAD FSVLIWDICS KYTPDIVPME K VKLSAGET ETTLLVTKPL YELGQNDACL SLCWLPRDQK LLLAGMHRNL AIFDLRNTSQ KMFVNTKAVQ GVTVDPYFHD RV ASFYEGQ VAIWDLRKFE KPVLTLTEQP KPLTKVAWCP TRTGLLATLT RDSNIIRLYD MQHTPTPIGD ETEPTIIERS VQP CDNYIA SFAWHPTSQN RMIVVTPNRT MSDFTVFERI SLAWSPITSL MWACGRHLYE CTEEENDNSL EKDIATKMRL RALS RYGLD TEQVWRNHIL AGNEDPQLKS LWYTLHFMKQ YTEDMDQKSP GNKGSLVYAG IKSIVKSSLG MVESSRHNWS GLDKQ SDIQ NLNEERILAL QLCGWIKKGT DVDVGPFLNS LVQEGEWERA AAVALFNLDI RRAIQILNEG ASSEKGDLNL NVVAMA LSG YTDEKNSLWR EMCSTLRLQL NNPYLCVMFA FLTSETGSYD GVLYENKVAV RDRVAFACKF LSDTQLNRYI EKLTNEM KE AGNLEGILLT GLTKDGVDLM ESYVDRTGDV QTASYCMLQG SPLDVLKDER VQYWIENYRN LLDAWRFWHK RAEFDIHR S KLDPSSKPLA QVFVSCNFCG KSISYSCSAV PHQGRGFSQY GVSGSPTKSK VTSCPGCRKP LPRCALCLIN MGTPVSSCP GGTKSDEKVD LSKDKKLAQF NNWFTWCHNC RHGGHAGHML SWFRDHAECP VSACTCKCMQ LDTTGNLVPA ETVQP

UniProtKB: GATOR2 complex protein MIOS

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Macromolecule #2: GATOR2 complex protein WDR24

MacromoleculeName: GATOR2 complex protein WDR24 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO / EC number: RING-type E3 ubiquitin transferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 88.326953 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MEKMSRVTTA LGGSVLTGRT MHCHLDAPAN AISVCRDAAQ VVVAGRSIFK IYAIEEEQFV EKLNLRVGRK PSLNLSCADV VWHQMDENL LATAATNGVV VTWNLGRPSR NKQDQLFTEH KRTVNKVCFH PTEAHVLLSG SQDGFMKCFD LRRKDSVSTF S GQSESVRD ...String:
MEKMSRVTTA LGGSVLTGRT MHCHLDAPAN AISVCRDAAQ VVVAGRSIFK IYAIEEEQFV EKLNLRVGRK PSLNLSCADV VWHQMDENL LATAATNGVV VTWNLGRPSR NKQDQLFTEH KRTVNKVCFH PTEAHVLLSG SQDGFMKCFD LRRKDSVSTF S GQSESVRD VQFSIRDYFT FASTFENGNV QLWDIRRPDR CERMFTAHNG PVFCCDWHPE DRGWLATGGR DKMVKVWDMT TH RAKEMHC VQTIASVARV KWRPECRHHL ATCSMMVDHN IYVWDVRRPF VPAAMFEEHR DVTTGIAWRH PHDPSFLLSG SKD SSLCQH LFRDASQPVE RANPEGLCYG LFGDLAFAAK ESLVAAESGR KPYTGDRRHP IFFKRKLDPA EPFAGLASSA LSVF ETEPG GGGMRWFVDT AERYALAGRP LAELCDHNAK VARELGRNQV AQTWTMLRII YCSPGLVPTA NLNHSVGKGG SCGLP LMNS FNLKDMAPGL GSETRLDRSK GDARSDTVLL DSSATLITNE DNEETEGSDV PADYLLGDVE GEEDELYLLD PEHAHP EDP ECVLPQEAFP LRHEIVDTPP GPEHLQDKAD SPHVSGSEAD VASLAPVDSS FSLLSVSHAL YDSRLPPDFF GVLVRDM LH FYAEQGDVQM AVSVLIVLGE RVRKDIDEQT QEHWYTSYID LLQRFRLWNV SNEVVKLSTS RAVSCLNQAS TTLHVNCS H CKRPMSSRGW VCDRCHRCAS MCAVCHHVVK GLFVWCQGCS HGGHLQHIMK WLEGSSHCPA GCGHLCEYS

UniProtKB: GATOR2 complex protein WDR24

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Macromolecule #3: GATOR2 complex protein WDR59

MacromoleculeName: GATOR2 complex protein WDR59 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 109.938391 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MAARWSSENV VVEFRDSQAT AMSVDCLGQH AVLSGRRFLY IVNLDAPFEG HRKISRQSKW DIGAVQWNPH DSFAHYFAAS SNQRVDLYK WKDGSGEVGT TLQGHTRVIS DLDWAVFEPD LLVTSSVDTY IYIWDIKDTR KPTVALSAVA GASQVKWNKK N ANCLATSH ...String:
MAARWSSENV VVEFRDSQAT AMSVDCLGQH AVLSGRRFLY IVNLDAPFEG HRKISRQSKW DIGAVQWNPH DSFAHYFAAS SNQRVDLYK WKDGSGEVGT TLQGHTRVIS DLDWAVFEPD LLVTSSVDTY IYIWDIKDTR KPTVALSAVA GASQVKWNKK N ANCLATSH DGDVRIWDKR KPSTAVEYLA AHLSKIHGLD WHPDSEHILA TSSQDNSVKF WDYRQPRKYL NILPCQVPVW KA RYTPFSN GLVTVMVPQL RRENSLLLWN VFDLNTPVHT FVGHDDVVLE FQWRKQKEGS KDYQLVTWSR DQTLRMWRVD SQM QRLCAN DILDGVDEFI ESISLLPEPE KTLHTEDTDH QHTASHGEEE ALKEDPPRNL LEERKSDQLG LPQTLQQEFS LINV QIRNV NVEMDAADRS CTVSVHCSNH RVKMLVKFPA QYPNNAAPSF QFINPTTITS TMKAKLLKIL KDTALQKVKR GQSCL EPCL RQLVSCLESF VNQEDSASSN PFALPNSVTP PLPTFARVTT AYGSYQDANI PFPRTSGARF CGAGYLVYFT RPMTMH RAV SPTEPTPRSL SALSAYHTGL IAPMKIRTEA PGNLRLYSGS PTRSEKEQVS ISSFYYKERK SRRWKSKREG SDSGNRQ IK AAGKVIIQDI ACLLPVHKSL GELYILNVND IQETCQKNAA SALLVGRKDL VQVWSLATVA TDLCLGPKSD PDLETPWA R HPFGRQLLES LLAHYCRLRD VQTLAMLCSV FEAQSRPQGL PNPFGPFPNR SSNLVVSHSR YPSFTSSGSC SSMSDPGLN TGGWNIAGRE AEHLSSPWGE SSPEELRFGS LTYSDPRERE RDQHDKNKRL LDPANTQQFD DFKKCYGEIL YRWGLREKRA EVLKFVSCP PDPHKGIEFG VYCSHCRSEV RGTQCAICKG FTFQCAICHV AVRGSSNFCL TCGHGGHTSH MMEWFRTQEV C PTGCGCHC LLESTF

UniProtKB: GATOR2 complex protein WDR59

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Macromolecule #4: Isoform B of Nucleoporin SEH1

MacromoleculeName: Isoform B of Nucleoporin SEH1 / type: protein_or_peptide / ID: 4 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 46.636289 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MFVARSIAAD HKDLIHDVSF DFHGRRMATC SSDQSVKVWD KSESGDWHCT ASWKTHSGSV WRVTWAHPEF GQVLASCSFD RTAAVWEEI VGESNDKLRG QSHWVKRTTL VDSRTSVTDV KFAPKHMGLM LATCSADGIV RIYEAPDVMN LSQWSLQHEI S CKLSCSCI ...String:
MFVARSIAAD HKDLIHDVSF DFHGRRMATC SSDQSVKVWD KSESGDWHCT ASWKTHSGSV WRVTWAHPEF GQVLASCSFD RTAAVWEEI VGESNDKLRG QSHWVKRTTL VDSRTSVTDV KFAPKHMGLM LATCSADGIV RIYEAPDVMN LSQWSLQHEI S CKLSCSCI SWNPSSSRAH SPMIAVGSDD SSPNAMAKVQ IFEYNENTRK YAKAETLMTV TDPVHDIAFA PNLGRSFHIL AI ATKDVRI FTLKPVRKEL TSSGGPTKFE IHIVAQFDNH NSQVWRVSWN ITGTVLASSG DDGCVRLWKA NYMDNWKCTG ILK GNGSPV NGSSQQGTSN PSLGSTIPSL QNSLNGSSAG RYFFTPLDSP RAGSRWSSYA QLLPPPPPPL VEHSCDADTA NLQY PHPRR RYLSRPLNPL PENEGI

UniProtKB: Nucleoporin SEH1

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Macromolecule #5: Isoform 3 of Protein SEC13 homolog

MacromoleculeName: Isoform 3 of Protein SEC13 homolog / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 40.791668 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MREPVLTWCV PLELLCSHPL PLSAFLKSQV KLYTYRACAG KDEMGKMVSV INTVDTSHED MIHDAQMDYY GTRLATCSSD RSVKIFDVR NGGQILIADL RGHEGPVWQV AWAHPMYGNI LASCSYDRKV IIWREENGTW EKSHEHAGHD SSVNSVCWAP H DYGLILAC ...String:
MREPVLTWCV PLELLCSHPL PLSAFLKSQV KLYTYRACAG KDEMGKMVSV INTVDTSHED MIHDAQMDYY GTRLATCSSD RSVKIFDVR NGGQILIADL RGHEGPVWQV AWAHPMYGNI LASCSYDRKV IIWREENGTW EKSHEHAGHD SSVNSVCWAP H DYGLILAC GSSDGAISLL TYTGEGQWEV KKINNAHTIG CNAVSWAPAV VPGSLIDHPS GQKPNYIKRF ASGGCDNLIK LW KEEEDGQ WKEEQKLEAH SDWVRDVAWA PSIGLPTSTI ASCSQDGRVF IWTCDDASSN TWSPKLLHKF NDVVWHVSWS ITA NILAVS GGDNKVTLWK ESVDGQWVCI SDVNKGQGSV SASVTEGQQN EQ

UniProtKB: Protein SEC13 homolog

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Macromolecule #6: Cytosolic arginine sensor for mTORC1 subunit 1

MacromoleculeName: Cytosolic arginine sensor for mTORC1 subunit 1 / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 36.265234 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MELHILEHRV RVLSVARPGL WLYTHPLIKL LFLPRRSRCK FFSLTETPED YTLMVDEEGF KELPPSEFLQ VAEATWLVLN VSSHSGAAV QAAGVTKIAR SVIAPLAEHH VSVLMLSTYQ TDFILVREQD LSVVIHTLAQ EFDIYREVGG EPVPVTRDDS S NGFPRTQH ...String:
MELHILEHRV RVLSVARPGL WLYTHPLIKL LFLPRRSRCK FFSLTETPED YTLMVDEEGF KELPPSEFLQ VAEATWLVLN VSSHSGAAV QAAGVTKIAR SVIAPLAEHH VSVLMLSTYQ TDFILVREQD LSVVIHTLAQ EFDIYREVGG EPVPVTRDDS S NGFPRTQH GPSPTVHPIQ SPQNRFCVLT LDPETLPAIA TTLIDVLFYS HSTPKEAASS SPEPSSITFF AFSLIEGYIS IV MDAETQK KFPSDLLLTS SSGELWRMVR IGGQPLGFDE CGIVAQIAGP LAAADISAYY ISTFNFAHAL VPEDGIGSVI EVL QRRQEG LAS

UniProtKB: Cytosolic arginine sensor for mTORC1 subunit 1

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Macromolecule #7: Sestrin-2

MacromoleculeName: Sestrin-2 / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
EC number: Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 54.544566 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MIVADSECRA ELKDYLRFAP GGVGDSGPGE EQRESRARRG PRGPSAFIPV EEVLREGAES LEQHLGLEAL MSSGRVDNLA VVMGLHPDY FTSFWRLHYL LLHTDGPLAS SWRHYIAIMA AARHQCSYLV GSHMAEFLQT GGDPEWLLGL HRAPEKLRKL S EINKLLAH ...String:
MIVADSECRA ELKDYLRFAP GGVGDSGPGE EQRESRARRG PRGPSAFIPV EEVLREGAES LEQHLGLEAL MSSGRVDNLA VVMGLHPDY FTSFWRLHYL LLHTDGPLAS SWRHYIAIMA AARHQCSYLV GSHMAEFLQT GGDPEWLLGL HRAPEKLRKL S EINKLLAH RPWLITKEHI QALLKTGEHT WSLAELIQAL VLLTHCHSLS SFVFGCGILP EGDADGSPAP QAPTPPSEQS SP PSRDPLN NSGGFESARD VEALMERMQQ LQESLLRDEG TSQEEMESRF ELEKSESLLV TPSADILEPS PHPDMLCFVE DPT FGYEDF TRRGAQAPPT FRAQDYTWED HGYSLIQRLY PEGGQLLDEK FQAAYSLTFN TIAMHSGVDT SVLRRAIWNY IHCV FGIRY DDYDYGEVNQ LLERNLKVYI KTVACYPEKT TRRMYNLFWR HFRHSEKVHV NLLLLEARMQ AALLYALRAI TRYMT

UniProtKB: Sestrin-2

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Macromolecule #8: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 8 / Number of copies: 32 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 48.87 e/Å2
Details: The total dose on the specimen was 48.87, 48.86 and 49.03 e-/A2 fractionated over 50 frames.
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: NONE
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

7uhy

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.41 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 586448
Initial angle assignmentType: OTHER
Final angle assignmentType: OTHER

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