+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-26519 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Title | Human GATOR2 complex | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Map data | COMPOSITE MAP. Sharpened. C2-pseudosymmetric. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sample |
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Function / homology | Function and homology information GATOR2 complex / Seh1-associated complex / protein exit from endoplasmic reticulum / COPII-coated vesicle budding / COPII-coated vesicle cargo loading / nuclear pore outer ring / nuclear pore organization / COPII vesicle coat / Nuclear Pore Complex (NPC) Disassembly / Amino acids regulate mTORC1 ...GATOR2 complex / Seh1-associated complex / protein exit from endoplasmic reticulum / COPII-coated vesicle budding / COPII-coated vesicle cargo loading / nuclear pore outer ring / nuclear pore organization / COPII vesicle coat / Nuclear Pore Complex (NPC) Disassembly / Amino acids regulate mTORC1 / Transport of Ribonucleoproteins into the Host Nucleus / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) / Transport of the SLBP independent Mature mRNA / attachment of mitotic spindle microtubules to kinetochore / Transport of the SLBP Dependant Mature mRNA / NS1 Mediated Effects on Host Pathways / SUMOylation of SUMOylation proteins / protein-containing complex localization / Transport of Mature mRNA Derived from an Intronless Transcript / Rev-mediated nuclear export of HIV RNA / SUMOylation of RNA binding proteins / Nuclear import of Rev protein / Transport of Mature mRNA derived from an Intron-Containing Transcript / NEP/NS2 Interacts with the Cellular Export Machinery / tRNA processing in the nucleus / Postmitotic nuclear pore complex (NPC) reformation / nucleocytoplasmic transport / COPII-mediated vesicle transport / Viral Messenger RNA Synthesis / mitotic metaphase chromosome alignment / SUMOylation of ubiquitinylation proteins / Vpr-mediated nuclear import of PICs / cellular response to nutrient levels / SUMOylation of DNA replication proteins / Regulation of HSF1-mediated heat shock response / positive regulation of TOR signaling / mRNA transport / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / SUMOylation of DNA damage response and repair proteins / nuclear pore / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / negative regulation of TORC1 signaling / positive regulation of TORC1 signaling / Resolution of Sister Chromatid Cohesion / MHC class II antigen presentation / cellular response to amino acid starvation / SUMOylation of chromatin organization proteins / HCMV Late Events / regulation of autophagy / RHO GTPases Activate Formins / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / Transcriptional regulation by small RNAs / intracellular protein transport / ER to Golgi transport vesicle membrane / ISG15 antiviral mechanism / kinetochore / autophagy / HCMV Early Events / Separation of Sister Chromatids / protein import into nucleus / protein transport / cell junction / nuclear envelope / snRNP Assembly / defense response to Gram-positive bacterium / cell division / lysosomal membrane / intracellular membrane-bounded organelle / endoplasmic reticulum membrane / SARS-CoV-2 activates/modulates innate and adaptive immune responses / structural molecule activity / extracellular exosome / nucleoplasm / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.66 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Authors | Rogala KB / Valenstein ML / Lalgudi PV | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Funding support | United States, 17 items
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Citation | Journal: Nature / Year: 2022 Title: Structure of the nutrient-sensing hub GATOR2. Authors: Max L Valenstein / Kacper B Rogala / Pranav V Lalgudi / Edward J Brignole / Xin Gu / Robert A Saxton / Lynne Chantranupong / Jonas Kolibius / Jan-Philipp Quast / David M Sabatini / Abstract: Mechanistic target of rapamycin complex 1 (mTORC1) controls growth by regulating anabolic and catabolic processes in response to environmental cues, including nutrients. Amino acids signal to mTORC1 ...Mechanistic target of rapamycin complex 1 (mTORC1) controls growth by regulating anabolic and catabolic processes in response to environmental cues, including nutrients. Amino acids signal to mTORC1 through the Rag GTPases, which are regulated by several protein complexes, including GATOR1 and GATOR2. GATOR2, which has five components (WDR24, MIOS, WDR59, SEH1L and SEC13), is required for amino acids to activate mTORC1 and interacts with the leucine and arginine sensors SESN2 and CASTOR1, respectively. Despite this central role in nutrient sensing, GATOR2 remains mysterious as its subunit stoichiometry, biochemical function and structure are unknown. Here we used cryo-electron microscopy to determine the three-dimensional structure of the human GATOR2 complex. We found that GATOR2 adopts a large (1.1 MDa), two-fold symmetric, cage-like architecture, supported by an octagonal scaffold and decorated with eight pairs of WD40 β-propellers. The scaffold contains two WDR24, four MIOS and two WDR59 subunits circularized via two distinct types of junction involving non-catalytic RING domains and α-solenoids. Integration of SEH1L and SEC13 into the scaffold through β-propeller blade donation stabilizes the GATOR2 complex and reveals an evolutionary relationship to the nuclear pore and membrane-coating complexes. The scaffold orients the WD40 β-propeller dimers, which mediate interactions with SESN2, CASTOR1 and GATOR1. Our work reveals the structure of an essential component of the nutrient-sensing machinery and provides a foundation for understanding the function of GATOR2 within the mTORC1 pathway. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
-Validation report
Summary document | emd_26519_validation.pdf.gz | 983.1 KB | Display | EMDB validaton report |
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Full document | emd_26519_full_validation.pdf.gz | 982.7 KB | Display | |
Data in XML | emd_26519_validation.xml.gz | 19.1 KB | Display | |
Data in CIF | emd_26519_validation.cif.gz | 21.8 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-26519 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-26519 | HTTPS FTP |
-Related structure data
Related structure data | 7uhyMC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_26519.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Annotation | COMPOSITE MAP. Sharpened. C2-pseudosymmetric. | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.0922 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
+Mask #1
+Mask #2
+Mask #3
+Mask #4
+Mask #5
+Mask #6
+Additional map: COMPOSITE MAP. Unsharpened. C2-pseudosymmetric. Used for the final...
+Additional map: LOCAL MAP #4. Sharpened. From C2-symmetry expanded particles.
+Additional map: LOCAL MAP #3. Sharpened. From C2-symmetry expanded particles.
+Additional map: LOCAL MAP #5. Sharpened.
+Additional map: LOCAL MAP #5. Unsharpened.
+Additional map: GLOBAL MAP. Sharpened. C2-symmetric.
+Additional map: GLOBAL MAP. Unsharpened. C2-symmetric.
+Additional map: LOCAL MAP #2. Unsharpened. From C2-symmetry expanded particles.
+Additional map: LOCAL MAP #1. Sharpened. From C2-symmetry expanded particles.
+Additional map: LOCAL MAP #1. Unsharpened. From C2-symmetry expanded particles.
+Additional map: LOCAL MAP #2. Sharpened. From C2-symmetry expanded particles.
+Additional map: LOCAL MAP #3. Unsharpened. From C2-symmetry expanded particles.
+Additional map: LOCAL MAP #4. Unsharpened. From C2-symmetry expanded particles.
+Half map: GLOBAL HALF-MAP B. C2-symmetric.
+Half map: GLOBAL HALF-MAP A. C2-symmetric.
-Sample components
-Entire : Human GATOR2
Entire | Name: Human GATOR2 |
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Components |
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-Supramolecule #1: Human GATOR2
Supramolecule | Name: Human GATOR2 / type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: #1-#7 Details: Purified five-component GATOR2 complex via a Flag-tag on MIOS. |
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Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: Homo sapiens (human) / Recombinant cell: HEK-293T |
Molecular weight | Theoretical: 1.1 MDa |
-Macromolecule #1: GATOR complex protein MIOS
Macromolecule | Name: GATOR complex protein MIOS / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 100.633383 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MEMDYKDDDD KGGGGGASTM SGTKPDILWA PHHVDRFVVC DSELSLYHVE STVNSELKAG SLRLSEDSAA TLLSINSDTP YMKCVAWYL NYDPECLLAV GQANGRVVLT SLGQDHNSKF KDLIGKEFVP KHARQCNTLA WNPLDSNWLA AGLDKHRADF S VLIWDICS ...String: MEMDYKDDDD KGGGGGASTM SGTKPDILWA PHHVDRFVVC DSELSLYHVE STVNSELKAG SLRLSEDSAA TLLSINSDTP YMKCVAWYL NYDPECLLAV GQANGRVVLT SLGQDHNSKF KDLIGKEFVP KHARQCNTLA WNPLDSNWLA AGLDKHRADF S VLIWDICS KYTPDIVPME KVKLSAGETE TTLLVTKPLY ELGQNDACLS LCWLPRDQKL LLAGMHRNLA IFDLRNTSQK MF VNTKAVQ GVTVDPYFHD RVASFYEGQV AIWDLRKFEK PVLTLTEQPK PLTKVAWCPT RTGLLATLTR DSNIIRLYDM QHT PTPIGD ETEPTIIERS VQPCDNYIAS FAWHPTSQNR MIVVTPNRTM SDFTVFERIS LAWSPITSLM WACGRHLYEC TEEE NDNSL EKDIATKMRL RALSRYGLDT EQVWRNHILA GNEDPQLKSL WYTLHFMKQY TEDMDQKSPG NKGSLVYAGI KSIVK SSLG MVESSRHNWS GLDKQSDIQN LNEERILALQ LCGWIKKGTD VDVGPFLNSL VQEGEWERAA AVALFNLDIR RAIQIL NEG ASSEKGDLNL NVVAMALSGY TDEKNSLWRE MCSTLRLQLN NPYLCVMFAF LTSETGSYDG VLYENKVAVR DRVAFAC KF LSDTQLNRYI EKLTNEMKEA GNLEGILLTG LTKDGVDLME SYVDRTGDVQ TASYCMLQGS PLDVLKDERV QYWIENYR N LLDAWRFWHK RAEFDIHRSK LDPSSKPLAQ VFVSCNFCGK SISYSCSAVP HQGRGFSQYG VSGSPTKSKV TSCPGCRKP LPRCALCLIN MGTPVSSCPG GTKSDEKVDL SKDKKLAQFN NWFTWCHNCR HGGHAGHMLS WFRDHAECPV SACTCKCMQL DTTGNLVPA ETVQP |
-Macromolecule #2: GATOR complex protein WDR24
Macromolecule | Name: GATOR complex protein WDR24 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 88.326953 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: 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 |
-Macromolecule #3: GATOR complex protein WDR59
Macromolecule | Name: GATOR complex protein WDR59 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 109.938391 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: 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 |
-Macromolecule #4: Isoform B of Nucleoporin SEH1
Macromolecule | Name: Isoform B of Nucleoporin SEH1 / type: protein_or_peptide / ID: 4 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 46.636289 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: 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 |
-Macromolecule #5: Protein SEC13 homolog
Macromolecule | Name: Protein SEC13 homolog / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 35.578438 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MVSVINTVDT SHEDMIHDAQ MDYYGTRLAT CSSDRSVKIF DVRNGGQILI ADLRGHEGPV WQVAWAHPMY GNILASCSYD RKVIIWREE NGTWEKSHEH AGHDSSVNSV CWAPHDYGLI LACGSSDGAI SLLTYTGEGQ WEVKKINNAH TIGCNAVSWA P AVVPGSLI ...String: MVSVINTVDT SHEDMIHDAQ MDYYGTRLAT CSSDRSVKIF DVRNGGQILI ADLRGHEGPV WQVAWAHPMY GNILASCSYD RKVIIWREE NGTWEKSHEH AGHDSSVNSV CWAPHDYGLI LACGSSDGAI SLLTYTGEGQ WEVKKINNAH TIGCNAVSWA P AVVPGSLI DHPSGQKPNY IKRFASGGCD NLIKLWKEEE DGQWKEEQKL EAHSDWVRDV AWAPSIGLPT STIASCSQDG RV FIWTCDD ASSNTWSPKL LHKFNDVVWH VSWSITANIL AVSGGDNKVT LWKESVDGQW VCISDVNKGQ GSVSASVTEG QQN EQ |
-Macromolecule #6: Unknown
Macromolecule | Name: Unknown / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 1.294587 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) |
-Macromolecule #7: Unknown
Macromolecule | Name: Unknown / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 698.854 Da |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) |
-Macromolecule #8: ZINC ION
Macromolecule | Name: ZINC ION / type: ligand / ID: 8 / Number of copies: 16 / Formula: ZN |
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Molecular weight | Theoretical: 65.409 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 3.0 mg/mL | ||||||||||||||||
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Buffer | pH: 7.5 Component:
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Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 1e-05 kPa | ||||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV | ||||||||||||||||
Details | 95% pure, monodisperse protein complex. Partial loss of a few subunits observed. Contaminating CCT chaperonin present. |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | #0 - Image recording ID: 1 / #0 - Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / #0 - Number grids imaged: 1 / #0 - Number real images: 4103 / #0 - Average exposure time: 2.4 sec. / #0 - Average electron dose: 44.0 e/Å2 #0 - Details: Movie stacks were recorded in super-resolution counting mode at the UMass Medical School's Cryo-EM Core Facility in Worcester, Massachusetts, USA. 30 frames per stack. #1 - Image recording ID: 2 / #1 - Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / #1 - Number grids imaged: 2 / #1 - Number real images: 28792 / #1 - Average exposure time: 4.0 sec. / #1 - Average electron dose: 47.0 e/Å2 #1 - Details: Movie stacks were recorded in super-resolution counting mode at MIT.nano in Cambridge, Massachusetts, USA. 30 frames per stack. |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 50.0 µm / Calibrated magnification: 45779 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 81000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Initial model |
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Details | Most of the structure was built de novo in Coot. WD40 propellers were rebuilt after fitting either deposited PDB coordinates of homologous structures or predicted models from RoseTTAFold. | ||||||||||
Refinement | Space: REAL / Protocol: OTHER / Overall B value: 182 | ||||||||||
Output model | PDB-7uhy: |