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- EMDB-27435: Active FLCN GAP complex -

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Basic information

Entry
Database: EMDB / ID: EMD-27435
TitleActive FLCN GAP complex
Map data
Sample
  • Complex: Cryo-EM structure of the Active FLCN GAP compex
    • Complex: Rag-Ragulator
      • Protein or peptide: x 7 types
    • Complex: FLCN:SLC-FNIP2
      • Protein or peptide: x 2 types
    • Protein or peptide: x 1 types
  • Ligand: x 3 types
Function / homology
Function and homology information


asparagine transport / L-asparagine transmembrane transporter activity / sterol sensor activity / negative regulation of cell proliferation involved in kidney development / L-arginine transmembrane transport / L-arginine transmembrane transporter activity / negative regulation of post-translational protein modification / cell proliferation involved in kidney development / regulation of cholesterol import / positive regulation of protein localization to lysosome ...asparagine transport / L-asparagine transmembrane transporter activity / sterol sensor activity / negative regulation of cell proliferation involved in kidney development / L-arginine transmembrane transport / L-arginine transmembrane transporter activity / negative regulation of post-translational protein modification / cell proliferation involved in kidney development / regulation of cholesterol import / positive regulation of protein localization to lysosome / regulation of cell-substrate junction organization / glutamine transport / L-glutamine transmembrane transporter activity / Gtr1-Gtr2 GTPase complex / regulation of cholesterol efflux / positive regulation of RNA polymerase II regulatory region sequence-specific DNA binding / L-amino acid transmembrane transporter activity / FNIP-folliculin RagC/D GAP / Ragulator complex / negative regulation of brown fat cell differentiation / regulation of Ras protein signal transduction / L-leucine transmembrane transporter activity / amino acid transmembrane transport / protein localization to cell junction / regulation of TORC1 signaling / negative regulation of lysosome organization / regulation of pro-B cell differentiation / amino acid transmembrane transporter activity / protein localization to lysosome / TORC1 signaling / regulation of TOR signaling / endosome organization / ATPase inhibitor activity / MTOR signalling / Amino acids regulate mTORC1 / fibroblast migration / lysosome localization / Energy dependent regulation of mTOR by LKB1-AMPK / protein localization to membrane / kinase activator activity / enzyme-substrate adaptor activity / negative regulation of glycolytic process / enzyme inhibitor activity / negative regulation of TOR signaling / arginine binding / cell-cell junction assembly / negative regulation of cold-induced thermogenesis / negative regulation of Rho protein signal transduction / azurophil granule membrane / endosomal transport / regulation of cell size / Macroautophagy / small GTPase-mediated signal transduction / lysosome organization / cholesterol binding / positive regulation of transforming growth factor beta receptor signaling pathway / RHOJ GTPase cycle / RHOQ GTPase cycle / mTORC1-mediated signalling / cellular response to nutrient levels / tertiary granule membrane / CDC42 GTPase cycle / glutathione transferase / RHOH GTPase cycle / hemopoiesis / ficolin-1-rich granule membrane / centriolar satellite / glutathione transferase activity / RHOG GTPase cycle / positive regulation of TOR signaling / regulation of receptor recycling / TOR signaling / RAC2 GTPase cycle / RAC3 GTPase cycle / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / response to amino acid / positive regulation of autophagy / specific granule membrane / energy homeostasis / positive regulation of intrinsic apoptotic signaling pathway / protein-membrane adaptor activity / positive regulation of TORC1 signaling / tumor necrosis factor-mediated signaling pathway / RAC1 GTPase cycle / ERK1 and ERK2 cascade / cellular response to amino acid starvation / cellular response to starvation / negative regulation of autophagy / viral genome replication / intrinsic apoptotic signaling pathway / RNA splicing / glutathione metabolic process / phosphatidylinositol 3-kinase/protein kinase B signal transduction / GTPase activator activity / transforming growth factor beta receptor signaling pathway / guanyl-nucleotide exchange factor activity / epithelial cell proliferation / Regulation of PTEN gene transcription / positive regulation of interleukin-8 production / cholesterol homeostasis
Similarity search - Function
Amino acid transporter, transmembrane domain / Folliculin / Folliculin, DENN domain / Folliculin, DENN domain, C-terminal superfamily / Transmembrane amino acid transporter protein / Folliculin C-terminal domain / Folliculin-interacting protein family / Folliculin-interacting protein, N-terminal domain / Folliculin-interacting protein, middle domain / Folliculin-interacting protein, C-terminal domain ...Amino acid transporter, transmembrane domain / Folliculin / Folliculin, DENN domain / Folliculin, DENN domain, C-terminal superfamily / Transmembrane amino acid transporter protein / Folliculin C-terminal domain / Folliculin-interacting protein family / Folliculin-interacting protein, N-terminal domain / Folliculin-interacting protein, middle domain / Folliculin-interacting protein, C-terminal domain / Folliculin-interacting protein N-terminus / Folliculin-interacting protein middle domain / Folliculin-interacting protein C-terminus / Tripartite DENN domain, FNIP1/2-type / Tripartite DENN FNIP1/2-type domain profile. / Folliculin/SMCR8, longin domain / Folliculin/SMCR8, tripartite DENN domain / Vesicle coat protein involved in Golgi to plasma membrane transport / Tripartite DENN FLCN/SMCR8-type domain profile. / LAMTOR1/MEH1 / Late endosomal/lysosomal adaptor and MAPK and MTOR activator / Late endosomal/lysosomal adaptor and MAPK and MTOR activator / Ragulator complex protein LAMTOR4 / Ragulator complex protein LAMTOR3 / Ragulator complex protein LAMTOR5 / RagA/B / Mitogen-activated protein kinase kinase 1 interacting / Ragulator complex protein LAMTOR5 / Mitogen-activated protein kinase kinase 1 interacting / Gtr1/RagA G protein / RagC/D / Gtr1/RagA G protein conserved region / Ragulator complex protein LAMTOR2-like / Roadblock/LAMTOR2 domain / Roadblock/LC7 domain / Roadblock/LC7 domain / Glutathione S-transferase, C-terminal domain / Glutathione S-transferase, N-terminal domain / Glutathione transferase family / Glutathione S-transferase, C-terminal / Soluble glutathione S-transferase N-terminal domain profile. / Glutathione S-transferase, C-terminal-like / Soluble glutathione S-transferase C-terminal domain profile. / Glutathione S-transferase, N-terminal / Glutathione S-transferase, C-terminal domain superfamily / Thioredoxin-like superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Ragulator complex protein LAMTOR5 / Glutathione S-transferase class-mu 26 kDa isozyme / Ragulator complex protein LAMTOR4 / Ragulator complex protein LAMTOR1 / Ras-related GTP-binding protein A / Neutral amino acid transporter 9 / Folliculin / Ras-related GTP-binding protein C / Folliculin-interacting protein 2 / Ragulator complex protein LAMTOR3 / Ragulator complex protein LAMTOR2
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.53 Å
AuthorsJansen RM / Hurley JH
Funding support United States, Italy, 4 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM111730 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM130995 United States
National Science Foundation (NSF, United States) United States
Italian Association for Cancer Research Italy
CitationJournal: Sci Adv / Year: 2022
Title: Structural basis for FLCN RagC GAP activation in MiT-TFE substrate-selective mTORC1 regulation.
Authors: Rachel M Jansen / Roberta Peruzzo / Simon A Fromm / Adam L Yokom / Roberto Zoncu / James H Hurley /
Abstract: The mechanistic target of rapamycin complex 1 (mTORC1) regulates cell growth and catabolism in response to nutrients through phosphorylation of key substrates. The tumor suppressor folliculin (FLCN) ...The mechanistic target of rapamycin complex 1 (mTORC1) regulates cell growth and catabolism in response to nutrients through phosphorylation of key substrates. The tumor suppressor folliculin (FLCN) is a RagC/D guanosine triphosphatase (GTPase)-activating protein (GAP) that regulates mTORC1 phosphorylation of MiT-TFE transcription factors, controlling lysosome biogenesis and autophagy. We determined the cryo-electron microscopy structure of the active FLCN complex (AFC) containing FLCN, FNIP2, the N-terminal tail of SLC38A9, the RagA:RagC GTPase dimer, and the Ragulator scaffold. Relative to the inactive lysosomal FLCN complex structure, FLCN reorients by 90°, breaks contact with RagA, and makes previously unseen contacts with RagC that position its Arg finger for catalysis. Disruption of the AFC-specific interfaces of FLCN and FNIP2 with RagC eliminated GAP activity and led to nuclear retention of TFE3, with no effect on mTORC1 substrates S6K or 4E-BP1. The structure provides a basis for regulation of an mTORC1 substrate-specific pathway and a roadmap to discover MiT-TFE family selective mTORC1 antagonists.
History
DepositionJun 25, 2022-
Header (metadata) releaseSep 28, 2022-
Map releaseSep 28, 2022-
UpdateSep 28, 2022-
Current statusSep 28, 2022Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_27435.png

Downloads & links

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Map

FileDownload / File: emd_27435.map.gz / Format: CCP4 / Size: 325 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.048 Å
Density
Contour LevelBy AUTHOR: 0.48
Minimum - Maximum-1.1009892 - 2.0484495
Average (Standard dev.)-0.0013066541 (±0.044274867)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions440440440
Spacing440440440
CellA=B=C: 461.12 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: Focused refinement at FLCN:RagC interface

Fileemd_27435_additional_1.map
AnnotationFocused refinement at FLCN:RagC interface
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_27435_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_27435_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Sample components

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Entire : Cryo-EM structure of the Active FLCN GAP compex

EntireName: Cryo-EM structure of the Active FLCN GAP compex
Components
  • Complex: Cryo-EM structure of the Active FLCN GAP compex
    • Complex: Rag-Ragulator
      • Protein or peptide: Ras-related GTP-binding protein C
      • Protein or peptide: Ras-related GTP-binding protein A
      • Protein or peptide: Ragulator complex protein LAMTOR1
      • Protein or peptide: Ragulator complex protein LAMTOR2
      • Protein or peptide: Ragulator complex protein LAMTOR3
      • Protein or peptide: Ragulator complex protein LAMTOR4
      • Protein or peptide: Ragulator complex protein LAMTOR5
    • Complex: FLCN:SLC-FNIP2
      • Protein or peptide: Folliculin-interacting protein 2
      • Protein or peptide: Folliculin
    • Protein or peptide: Glutathione S-transferase class-mu 26 kDa isozyme,Sodium-coupled neutral amino acid transporter 9 chimera
  • Ligand: [(2~{R},3~{S},4~{R},5~{R})-5-[2,6-bis(oxidanylidene)-3~{H}-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphono hydrogen phosphate
  • Ligand: BERYLLIUM TRIFLUORIDE ION
  • Ligand: GUANOSINE-5'-DIPHOSPHATE

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Supramolecule #1: Cryo-EM structure of the Active FLCN GAP compex

SupramoleculeName: Cryo-EM structure of the Active FLCN GAP compex / type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: #1-#10
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #2: Rag-Ragulator

SupramoleculeName: Rag-Ragulator / type: complex / Chimera: Yes / ID: 2 / Parent: 1 / Macromolecule list: #1-#7
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)

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Supramolecule #3: FLCN:SLC-FNIP2

SupramoleculeName: FLCN:SLC-FNIP2 / type: complex / Chimera: Yes / ID: 3 / Parent: 1 / Macromolecule list: #9-#10
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)

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Macromolecule #1: Ras-related GTP-binding protein C

MacromoleculeName: Ras-related GTP-binding protein C / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
EC number: Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 44.384004 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSLQYGAEET PLAGSYGAAD SFPKDFGYGV EEEEEEAAAA GGGVGAGAGG GCGPGGADSS KPRILLMGLR RSGKSSIQKV VFHKMSPNE TLFLESTNKI YKDDISNSSF VNFQIWDFPG QMDFFDPTFD YEMIFRGTGA LIYVIDAQDD YMEALTRLHI T VSKAYKVN ...String:
MSLQYGAEET PLAGSYGAAD SFPKDFGYGV EEEEEEAAAA GGGVGAGAGG GCGPGGADSS KPRILLMGLR RSGKSSIQKV VFHKMSPNE TLFLESTNKI YKDDISNSSF VNFQIWDFPG QMDFFDPTFD YEMIFRGTGA LIYVIDAQDD YMEALTRLHI T VSKAYKVN PDMNFEVFIH KVNGLSDDHK IETQRDIHQR ANDDLADAGL EKLHLSFYLT SIYDHSIFEA FSKVVQKLIP QL PTLENLL NIFISNSGIE KAFLFDVVSK IYIATDSSPV DMQSYELCCD MIDVVIDVSC IYGLKEDGSG SAYDKESMAI IKL NNTTVL YLKEVTKFLA LVCILREESF ERKGLIDYNF HCFRKAIHEV FEVGVTSHRS CGHQTSASSL KALTHNGTPR NAIL

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Macromolecule #2: Ras-related GTP-binding protein A

MacromoleculeName: Ras-related GTP-binding protein A / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 39.362078 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MSWSHPQFEK GGFDIDYKDD DDKMPNTAMK KKVLLMGKSG SGKTSMRSII FANYIARDTR RLGATIDVEH SHVRFLGNLV LNLWDCGGQ DTFMENYFTS QRDNIFRNVE VLIYVFDVES RELEKDMHYY QSCLEAILQN SPDAKIFCLV HKMDLVQEDQ R DLIFKERE ...String:
MSWSHPQFEK GGFDIDYKDD DDKMPNTAMK KKVLLMGKSG SGKTSMRSII FANYIARDTR RLGATIDVEH SHVRFLGNLV LNLWDCGGQ DTFMENYFTS QRDNIFRNVE VLIYVFDVES RELEKDMHYY QSCLEAILQN SPDAKIFCLV HKMDLVQEDQ R DLIFKERE EDLRRLSRPL ECACFRTSIW DETLYKAWSS IVYQLIPNVQ QLEMNLRNFA QIIEADEVLL FERATFLVIS HY QCKEQRD VHRFEKISNI IKQFKLSCSK LAASFQSMEV RNSNFAAFID IFTSNTYVMV VMSDPSIPSA ATLINIRNAR KHF EKLERV DGPKHSLLMR

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Macromolecule #3: Ragulator complex protein LAMTOR1

MacromoleculeName: Ragulator complex protein LAMTOR1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 18.32535 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
SNAEFMACCY SSENEDSDQD REERKLLLDP SSPPTKALNG AEPNYHSLPS ARTDEQALLS SILAKTASNI IDVSAADSQG MEQHEYMDR ARQYSTRLAV LSSSLTHWKK LPPLPSLTSQ PHQVLASEPI PFSDLQQVSR IAAYAYSALS QIRVDAKEEL V VQFGIP

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Macromolecule #4: Ragulator complex protein LAMTOR2

MacromoleculeName: Ragulator complex protein LAMTOR2 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.645579 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
GAMLRPKALT QVLSQANTGG VQSTLLLNNE GSLLAYSGYG DTDARVTAAI ASNIWAAYDR NGNQAFNEDN LKFILMDCME GRVAITRVA NLLLCMYAKE TVGFGMLKAK AQALVQYLEE PLTQVAAS

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Macromolecule #5: Ragulator complex protein LAMTOR3

MacromoleculeName: Ragulator complex protein LAMTOR3 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.637678 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MADDLKRFLY KKLPSVEGLH AIVVSDRDGV PVIKVANDNA PEHALRPGFL STFALATDQG SKLGLSKNKS IICYYNTYQV VQFNRLPLV VSFIASSSAN TGLIVSLEKE LAPLFEELRQ VVEVS

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Macromolecule #6: Ragulator complex protein LAMTOR4

MacromoleculeName: Ragulator complex protein LAMTOR4 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 10.753236 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MTSALTQGLE RIPDQLGYLV LSEGAVLASS GDLENDEQAA SAISELVSTA CGFRLHRGMN VPFKRLSVVF GEHTLLVTVS GQRVFVVKR QNRGREPIDV

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Macromolecule #7: Ragulator complex protein LAMTOR5

MacromoleculeName: Ragulator complex protein LAMTOR5 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 18.17852 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MEPGAGHLDG HRAGSPSLRQ ALCDGSAVMF SSKERGRCTV INFVPLEAPL RSTPRSRQVT EACGGEGRAV PLGSEPEWSV GGMEATLEQ HLEDTMKNPS IVGVLCTDSQ GLNLGCRGTL SDEHAGVISV LAQQAAKLTS DPTDIPVVCL ESDNGNIMIQ K HDGITVAV HKMAS

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Macromolecule #8: Glutathione S-transferase class-mu 26 kDa isozyme,Sodium-coupled ...

MacromoleculeName: Glutathione S-transferase class-mu 26 kDa isozyme,Sodium-coupled neutral amino acid transporter 9 chimera
type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO / EC number: glutathione transferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.000711 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MASPILGYWK IKGLVQPTRL LLEYLEEKYE EHLYERDEGD KWRNKKFELG LEFPNLPYYI DGDVKLTQSM AIIRYIADKH NMLGGCPKE RAEISMLEGA VLDIRYGVSR IAYSKDFETL KVDFLSKLPE MLKMFEDRLC HKTYLNGDHV THPDFMLYDA L DVVLYMDP ...String:
MASPILGYWK IKGLVQPTRL LLEYLEEKYE EHLYERDEGD KWRNKKFELG LEFPNLPYYI DGDVKLTQSM AIIRYIADKH NMLGGCPKE RAEISMLEGA VLDIRYGVSR IAYSKDFETL KVDFLSKLPE MLKMFEDRLC HKTYLNGDHV THPDFMLYDA L DVVLYMDP MCLDAFPKLV CFKKRIEAIP QIDKYLKSSK YIAWPLQGWQ ATFGGGDHPP KSDDYDIPTT ENLYFQGGTM AN MNSDSRH LGTSEVDHER DPGPMNIQFE PSDLRSKRPF CIEPTNIVNV NHVIQRVSDH ASAMNKRIHY YSRLTTPADK ALI APDHVV PAPEECYVYS PLGSAYKLQS YTEGYGKNTS

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Macromolecule #9: Folliculin-interacting protein 2

MacromoleculeName: Folliculin-interacting protein 2 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 149.865641 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MASPILGYWK IKGLVQPTRL LLEYLEEKYE EHLYERDEGD KWRNKKFELG LEFPNLPYYI DGDVKLTQSM AIIRYIADKH NMLGGCPKE RAEISMLEGA VLDIRYGVSR IAYSKDFETL KVDFLSKLPE MLKMFEDRLC HKTYLNGDHV THPDFMLYDA L DVVLYMDP ...String:
MASPILGYWK IKGLVQPTRL LLEYLEEKYE EHLYERDEGD KWRNKKFELG LEFPNLPYYI DGDVKLTQSM AIIRYIADKH NMLGGCPKE RAEISMLEGA VLDIRYGVSR IAYSKDFETL KVDFLSKLPE MLKMFEDRLC HKTYLNGDHV THPDFMLYDA L DVVLYMDP MCLDAFPKLV CFKKRIEAIP QIDKYLKSSK YIAWPLQGWQ ATFGGGDHPP KSDDYDIPTT ENLYFQGGTM AP TLLQKLF NKRGSSGSSA AASAQGRAPK EGPAFSWSCS EFDLNEIRLI VYQDCDRRGR QVLFDSKAVQ KIEEVTAQKT EDV PIKISA KCCQGSSSVS SSSSSSISSH SSSGGSSHHA KEQLPKYQYT RPASDVNMLG EMMFGSVAMS YKGSTLKIHY IRSP PQLMI SKVFSARMGS FCGSTNNLQD SFEYINQDPN LGKLNTNQNS LGPCRTGSNL AHSTPVDMPS RGQNEDRDSG IARSA SLSS LLITPFPSPS SSTSSSSSYQ RRWLRSQTTS LENGIIPRRS TDETFSLAEE TCSSNPAMVR RKKIAISIIF SLCEKE EAQ RNFQDFFFSH FPLFESHMNR LKSAIEKAMI SCRKIAESSL RVQFYVSRLM EALGEFRGTI WNLYSVPRIA EPVWLTM MS GTLEKNQLCQ RFLKEFTLLI EQINKNQFFA ALLTAVLTYH LAWVPTVMPV DHPPIKAFSE KRTSQSVNML AKTHPYNP L WAQLGDLYGA IGSPVRLTRT VVVGKQKDLV QRILYVLTYF LRCSELQENQ LTWSGNHGEG DQVLNGSKII TALEKGEVE ESEYVVITVR NEPALVPPIL PPTAAERHNP WPTGFPECPE GTDSRDLGLK PDKEANRRPE QGSEACSAGC LGPASDASWK PQNAFCGDE KNKEAPQDGS SRLPSCEVLG AGMKMDQQAV CELLKVEMPT RLPDRSVAWP CPDRHLREKP SLEKVTFQIG S FASPESDF ESRMKKMEER VKACGPSLEA SEAADVAQDP QVSRSPFKPG FQENVCCPQN RLSEGDEGES DKGFAEDRGS RN DMAADIA GQLSHAADLG TASHGAGGTG GRRLEATRGL YVKAAEGPVL EPVAPRCVQR GPGLVAGANI PCGDDNKKAN FRT EGDIPR NESSDSALGD SDDEACASAM LDLGHGGDRT GGSLEVELPL PRSQSISTQN VRNFGRSLLA GYCPTYMPDL VLHG TGSDE KLKQCLVADL VHTVHHPVLD EPIAEAVCII ADTDKWSVQV ATSQRKVTDN MKLGQDVLVS SQVSSLLQSI LQLYK LHLP ADFCIMHLED RLQEMYLKSK MLSEYLRGHT RVHVKELGVV LGIESNDLPL LTAIASTHSP YVAQILL

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Macromolecule #10: Folliculin

MacromoleculeName: Folliculin / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 69.14307 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MASWSHPQFE KGGGARGGSG GGSWSHPQFE KGFDYKDDDD KGTMNAIVAL CHFCELHGPR TLFCTEVLHA PLPQGDGNED SPGQGEQAE EEEGGIQMNS RMRAHSPAEG ASVESSSPGP KKSDMCEGCR SLAAGHPGYI SHDKETSIKY VSHQHPSHPQ L FSIVRQAC ...String:
MASWSHPQFE KGGGARGGSG GGSWSHPQFE KGFDYKDDDD KGTMNAIVAL CHFCELHGPR TLFCTEVLHA PLPQGDGNED SPGQGEQAE EEEGGIQMNS RMRAHSPAEG ASVESSSPGP KKSDMCEGCR SLAAGHPGYI SHDKETSIKY VSHQHPSHPQ L FSIVRQAC VRSLSCEVCP GREGPIFFGD EQHGFVFSHT FFIKDSLARG FQRWYSIITI MMDRIYLINS WPFLLGKVRG II DELQGKA LKVFEAEQFG CPQRAQRMNT AFTPFLHQRN GNAARSLTSL TSDDNLWACL HTSFAWLLKA CGSRLTEKLL EGA PTEDTL VQMEKLADLE EESESWDNSE AEEEEKAPVL PESTEGRELT QGPAESSSLS GCGSWQPRKL PVFKSLRHMR QVLG APSFR MLAWHVLMGN QVIWKSRDVD LVQSAFEVLR TMLPVGCVRI IPYSSQYEEA YRCNFLGLSP HVQIPPHVLS SEFAV IVEV HAAARSTLHP VGCEDDQSLS KYEFVVTSGS PVAADRVGPT ILNKIEAALT NQNLSVDVVD QCLVCLKEEW MNKVKV LFK FTKVDSRPKE DTQKLLSILG ASEEDNVKLL KFWMTGLSKT YKSHLMSTVR SPTASESRN

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Macromolecule #11: [(2~{R},3~{S},4~{R},5~{R})-5-[2,6-bis(oxidanylidene)-3~{H}-purin-...

MacromoleculeName: [(2~{R},3~{S},4~{R},5~{R})-5-[2,6-bis(oxidanylidene)-3~{H}-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphono hydrogen phosphate
type: ligand / ID: 11 / Number of copies: 1 / Formula: CZC
Molecular weightTheoretical: 444.185 Da
Chemical component information

ChemComp-CZC:
[(2~{R},3~{S},4~{R},5~{R})-5-[2,6-bis(oxidanylidene)-3~{H}-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphono hydrogen phosphate

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Macromolecule #12: BERYLLIUM TRIFLUORIDE ION

MacromoleculeName: BERYLLIUM TRIFLUORIDE ION / type: ligand / ID: 12 / Number of copies: 1 / Formula: BEF
Molecular weightTheoretical: 66.007 Da
Chemical component information

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

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Macromolecule #13: GUANOSINE-5'-DIPHOSPHATE

MacromoleculeName: GUANOSINE-5'-DIPHOSPHATE / type: ligand / ID: 13 / Number of copies: 1 / Formula: GDP
Molecular weightTheoretical: 443.201 Da
Chemical component information

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

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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

Concentration1 mg/mL
BufferpH: 7.4
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

6wj2

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.53 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 177018
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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