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- EMDB-28376: Structure of a human EMC:human Cav1.2 channel complex in GDN dete... -

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Basic information

Entry
Database: EMDB / ID: EMD-28376
TitleStructure of a human EMC:human Cav1.2 channel complex in GDN detergent (ECAB Map 3)
Map dataStructure of a human EMC:human Cav1.2 channel complex in GDN detergent (ECAB Map 3)
Sample
  • Complex: Ternary complex of the human ER membrane protein complex (EMC) with human CaV alpha1C and rabbit CaV beta3
    • Complex: Human CaV alpha1C
      • Protein or peptide: x 1 types
    • Complex: ER membrane protein complex subunit 1Endoplasmic reticulum
      • Protein or peptide: x 1 types
    • Complex: Rabbit CaV beta3
      • Protein or peptide: x 1 types
    • Protein or peptide: x 8 types
  • Ligand: x 2 types
Keywordsendoplasmic reticulum membrane protein complex / voltage-gated calcium channel / holdase / biogenesis / MEMBRANE PROTEIN
Function / homology
Function and homology information


inorganic cation transmembrane transporter activity / extrinsic component of endoplasmic reticulum membrane / EMC complex / omegasome membrane / : / protein insertion into ER membrane by stop-transfer membrane-anchor sequence / voltage-gated calcium channel activity involved in AV node cell action potential / voltage-gated calcium channel activity involved in cardiac muscle cell action potential / immune system development / magnesium ion transport ...inorganic cation transmembrane transporter activity / extrinsic component of endoplasmic reticulum membrane / EMC complex / omegasome membrane / : / protein insertion into ER membrane by stop-transfer membrane-anchor sequence / voltage-gated calcium channel activity involved in AV node cell action potential / voltage-gated calcium channel activity involved in cardiac muscle cell action potential / immune system development / magnesium ion transport / cobalt ion transmembrane transporter activity / positive regulation of high voltage-gated calcium channel activity / tail-anchored membrane protein insertion into ER membrane / membrane depolarization during atrial cardiac muscle cell action potential / Miscellaneous transport and binding events / Phase 2 - plateau phase / calcium ion transmembrane transport via high voltage-gated calcium channel / membrane depolarization during AV node cell action potential / magnesium ion transmembrane transporter activity / ferrous iron transmembrane transporter activity / positive regulation of adenylate cyclase activity / copper ion transport / cardiac conduction / L-type voltage-gated calcium channel complex / membrane depolarization during cardiac muscle cell action potential / regulation of ventricular cardiac muscle cell action potential / cardiac muscle cell action potential involved in contraction / high voltage-gated calcium channel activity / camera-type eye development / NCAM1 interactions / embryonic forelimb morphogenesis / calcium ion transport into cytosol / cell communication by electrical coupling involved in cardiac conduction / voltage-gated calcium channel complex / regulation of heart rate by cardiac conduction / Phase 0 - rapid depolarisation / alpha-actinin binding / calcium ion import across plasma membrane / calcium channel regulator activity / autophagosome assembly / RHOA GTPase cycle / voltage-gated calcium channel activity / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / positive regulation of endothelial cell proliferation / positive regulation of endothelial cell migration / Regulation of insulin secretion / calcium ion transmembrane transport / postsynaptic density membrane / Adrenaline,noradrenaline inhibits insulin secretion / Z disc / positive regulation of angiogenesis / heart development / positive regulation of cytosolic calcium ion concentration / perikaryon / early endosome membrane / carbohydrate binding / angiogenesis / postsynaptic density / early endosome / calmodulin binding / Golgi membrane / dendrite / apoptotic process / endoplasmic reticulum membrane / Golgi apparatus / endoplasmic reticulum / protein-containing complex / extracellular region / membrane / metal ion binding / plasma membrane / cytoplasm
Similarity search - Function
ER membrane protein complex subunit 8/9 / Uncharacterised protein family (UPF0172) / TMEM85/ER membrane protein complex subunit 4 / Protein of unknown function (DUF1077) / ER membrane protein complex subunit 7, beta-sandwich domain / ER membrane protein complex subunit 7 / ER membrane protein complex subunit 7, beta-sandwich domain / ER membrane protein complex subunit 6 / ER membrane protein complex subunit 3 / ER membrane protein complex subunit 1, C-terminal ...ER membrane protein complex subunit 8/9 / Uncharacterised protein family (UPF0172) / TMEM85/ER membrane protein complex subunit 4 / Protein of unknown function (DUF1077) / ER membrane protein complex subunit 7, beta-sandwich domain / ER membrane protein complex subunit 7 / ER membrane protein complex subunit 7, beta-sandwich domain / 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 / Voltage-dependent calcium channel, L-type, beta-3 subunit / Voltage-dependent L-type calcium channel subunit beta-3, SH3 domain / Voltage-dependent calcium channel, L-type, alpha-1C subunit / Voltage-dependent L-type calcium channel subunit beta-1-4, N-terminal A domain / Voltage-dependent calcium channel, L-type, beta subunit / Voltage gated calcium channel subunit beta domain 4Aa N terminal / Voltage-gated calcium channel subunit alpha, C-terminal / Voltage-gated calcium channel subunit alpha, C-term / Voltage-dependent calcium channel, L-type, alpha-1 subunit / Voltage-dependent calcium channel, alpha-1 subunit, IQ domain / Voltage gated calcium channel IQ domain / Voltage gated calcium channel IQ domain / Pyrrolo-quinoline quinone repeat / PQQ-like domain / Carbohydrate-binding-like fold / Voltage-dependent calcium channel, alpha-1 subunit / Tetratricopeptide repeat / Voltage-dependent L-type calcium channel, IQ-associated domain / Voltage-dependent L-type calcium channel, IQ-associated / Guanylate kinase/L-type calcium channel beta subunit / Guanylate kinase / Guanylate kinase homologues. / Quinoprotein alcohol dehydrogenase-like superfamily / Voltage-dependent channel domain superfamily / TPR repeat region circular profile. / TPR repeat profile. / MPN domain / MPN domain profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / SH3-like domain superfamily / Ion transport domain / Ion transport protein / Src homology 3 (SH3) domain profile. / SH3 domain / Tetratricopeptide-like helical domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ER membrane protein complex subunit 8 / Voltage-dependent L-type calcium channel subunit beta-3 / Voltage-dependent L-type calcium channel subunit alpha-1C / ER membrane protein complex subunit 2 / ER membrane protein complex subunit 4 / ER membrane protein complex subunit 10 / ER membrane protein complex subunit 5 / ER membrane protein complex subunit 1 / ER membrane protein complex subunit 6 / Endoplasmic reticulum membrane protein complex subunit 7 / ER membrane protein complex subunit 3
Similarity search - Component
Biological speciesHomo sapiens (human) / Oryctolagus cuniculus (rabbit)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsChen Z / Mondal A / Abderemane-Ali F / Minor DL
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)HL080050 United States
National Institutes of Health/National Institute on Deafness and Other Communication Disorders (NIH/NIDCD)DC007664 United States
CitationJournal: Nature / Year: 2023
Title: EMC chaperone-Ca structure reveals an ion channel assembly intermediate.
Authors: Zhou Chen / Abhisek Mondal / Fayal Abderemane-Ali / Seil Jang / Sangeeta Niranjan / José L Montaño / Balyn W Zaro / Daniel L Minor /
Abstract: Voltage-gated ion channels (VGICs) comprise multiple structural units, the assembly of which is required for function. Structural understanding of how VGIC subunits assemble and whether chaperone ...Voltage-gated ion channels (VGICs) comprise multiple structural units, the assembly of which is required for function. Structural understanding of how VGIC subunits assemble and whether chaperone proteins are required is lacking. High-voltage-activated calcium channels (Cas) are paradigmatic multisubunit VGICs whose function and trafficking are powerfully shaped by interactions between pore-forming Ca1 or Ca2 Caα (ref. ), and the auxiliary Caβ and Caαδ subunits. Here we present cryo-electron microscopy structures of human brain and cardiac Ca1.2 bound with Caβ to a chaperone-the endoplasmic reticulum membrane protein complex (EMC)-and of the assembled Ca1.2-Caβ-Caαδ-1 channel. These structures provide a view of an EMC-client complex and define EMC sites-the transmembrane (TM) and cytoplasmic (Cyto) docks; interaction between these sites and the client channel causes partial extraction of a pore subunit and splays open the Caαδ-interaction site. The structures identify the Caαδ-binding site for gabapentinoid anti-pain and anti-anxiety drugs, show that EMC and Caαδ interactions with the channel are mutually exclusive, and indicate that EMC-to-Caαδ hand-off involves a divalent ion-dependent step and Ca1.2 element ordering. Disruption of the EMC-Ca complex compromises Ca function, suggesting that the EMC functions as a channel holdase that facilitates channel assembly. Together, the structures reveal a Ca assembly intermediate and EMC client-binding sites that could have wide-ranging implications for the biogenesis of VGICs and other membrane proteins.
History
DepositionOct 3, 2022-
Header (metadata) releaseMay 24, 2023-
Map releaseMay 24, 2023-
UpdateJul 26, 2023-
Current statusJul 26, 2023Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_28376.png

Downloads & links

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Map

FileDownload / File: emd_28376.map.gz / Format: CCP4 / Size: 325 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationStructure of a human EMC:human Cav1.2 channel complex in GDN detergent (ECAB Map 3)
Voxel sizeX=Y=Z: 0.8466 Å
Density
Contour LevelBy AUTHOR: 5.93
Minimum - Maximum-11.47803 - 33.489620000000002
Average (Standard dev.)0.000022971937 (±1.0000407)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions440440440
Spacing440440440
CellA=B=C: 372.504 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Ternary complex of the human ER membrane protein complex (EMC) wi...

EntireName: Ternary complex of the human ER membrane protein complex (EMC) with human CaV alpha1C and rabbit CaV beta3
Components
  • Complex: Ternary complex of the human ER membrane protein complex (EMC) with human CaV alpha1C and rabbit CaV beta3
    • Complex: Human CaV alpha1C
      • Protein or peptide: Voltage-dependent L-type calcium channel subunit alpha-1C
    • Complex: ER membrane protein complex subunit 1Endoplasmic reticulum
      • Protein or peptide: ER membrane protein complex subunit 1Endoplasmic reticulum
    • Complex: Rabbit CaV beta3
      • Protein or peptide: Voltage-dependent L-type calcium channel subunit beta-3
    • Protein or peptide: ER membrane protein complex subunit 2Endoplasmic reticulum
    • Protein or peptide: ER membrane protein complex subunit 3Endoplasmic reticulum
    • Protein or peptide: ER membrane protein complex subunit 5Endoplasmic reticulum
    • Protein or peptide: ER membrane protein complex subunit 6Endoplasmic reticulum
    • Protein or peptide: ER membrane protein complex subunit 7Endoplasmic reticulum
    • Protein or peptide: ER membrane protein complex subunit 8Endoplasmic reticulum
    • Protein or peptide: ER membrane protein complex subunit 10Endoplasmic reticulum
    • Protein or peptide: ER membrane protein complex subunit 4Endoplasmic reticulum
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en

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Supramolecule #1: Ternary complex of the human ER membrane protein complex (EMC) wi...

SupramoleculeName: Ternary complex of the human ER membrane protein complex (EMC) with human CaV alpha1C and rabbit CaV beta3
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#11
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #2: Human CaV alpha1C

SupramoleculeName: Human CaV alpha1C / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #9
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 187 KDa

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Supramolecule #3: ER membrane protein complex subunit 1

SupramoleculeName: ER membrane protein complex subunit 1 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 112 KDa

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Supramolecule #4: Rabbit CaV beta3

SupramoleculeName: Rabbit CaV beta3 / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #10
Source (natural)Organism: Oryctolagus cuniculus (rabbit)
Molecular weightTheoretical: 100 KDa

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Macromolecule #1: ER membrane protein complex subunit 1

MacromoleculeName: ER membrane protein complex subunit 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 109.598438 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: AVYEDQVGKF DWRQQYVGKV KFASLEFSPG SKKLVVATEK NVIAALNSRT GEILWRHVDK GTAEGAVDAM LLHGQDVITV SNGGRIMRS WETNIGGLNW EITLDSGSFQ ALGLVGLQES VRYIAVLKKT TLALHHLSSG HLKWVEHLPE SDSIHYQMVY S YGSGVVWA ...String:
AVYEDQVGKF DWRQQYVGKV KFASLEFSPG SKKLVVATEK NVIAALNSRT GEILWRHVDK GTAEGAVDAM LLHGQDVITV SNGGRIMRS WETNIGGLNW EITLDSGSFQ ALGLVGLQES VRYIAVLKKT TLALHHLSSG HLKWVEHLPE SDSIHYQMVY S YGSGVVWA LGVVPFSHVN IVKFNVEDGE IVQQVRVSTP WLQHLSGACG VVDEAVLVCP DPSSRSLQTL ALETEWELRQ IP LQSLDLE FGSGFQPRVL PTQPNPVDAS RAQFFLHLSP SHYALLQYHY GTLSLLKNFP QTALVSFATT GEKTVAAVMA CRN EVQKSS SSEDGSMGSF SEKSSSKDSL ACFNQTYTIN LYLVETGRRL LDTTITFSLE QSGTRPERLY IQVFLKKDDS VGYR ALVQT EDHLLLFLQQ LAGKVVLWSR EESLAEVVCL EMVDLPLTGA QAELEGEFGK KADGLLGMFL KRLSSQLILL QAWTS HLWK MFYDARKPRS QIKNEINIDT LARDEFNLQK MMVMVTASGK LFGIESSSGT ILWKQYLPNV KPDSSFKLMV QRTTAH FPH PPQCTLLVKD KESGMSSLYV FNPIFGKWSQ VAPPVLKRPI LQSLLLPVMD QDYAKVLLLI DDEYKVTAFP ATRNVLR QL HELAPSIFFY LVDAEQGRLC GYRLRKDLTT ELSWELTIPP EVQRIVKVKG KRSSEHVHSQ GRVMGDRSVL YKSLNPNL L AVVTESTDAH HERTFIGIFL IDGVTGRIIH SSVQKKAKGP VHIVHSENWV VYQYWNTKAR RNEFTVLELY EGTEQYNAT AFSSLDRPQL PQVLQQSYIF PSSISAMEAT ITERGITSRH LLIGLPSGAI LSLPKALLDP RRPEIPTEQS REENLIPYSP DVQIHAERF INYNQTVSRM RGIYTAPSGL ESTCLVVAYG LDIYQTRVYP SKQFDVLKDD YDYVLISSVL FGLVFATMIT K RLAQVKLL NRAWR

UniProtKB: ER membrane protein complex subunit 1

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Macromolecule #2: ER membrane protein complex subunit 2

MacromoleculeName: ER membrane protein complex subunit 2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 34.250797 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: KVSELYDVTW EEMRDKMRKW REENSRNSEQ IVEVGEELIN EYASKLGDDI WIIYEQVMIA ALDYGRDDLA LFCLQELRRQ FPGSHRVKR LTGMRFEAME RYDDAIQLYD RILQEDPTNT AARKRKIAIR KAQGKNVEAI RELNEYLEQF VGDQEAWHEL A ELYINEHD ...String:
KVSELYDVTW EEMRDKMRKW REENSRNSEQ IVEVGEELIN EYASKLGDDI WIIYEQVMIA ALDYGRDDLA LFCLQELRRQ FPGSHRVKR LTGMRFEAME RYDDAIQLYD RILQEDPTNT AARKRKIAIR KAQGKNVEAI RELNEYLEQF VGDQEAWHEL A ELYINEHD YAKAAFCLEE LMMTNPHNHL YCQQYAEVKY TQGGLENLEL SRKYFAQALK LNNRNMRALF GLYMSASHIA SN PKASAKT KKDNMKYASW AASQINRAYQ FAGRSKKETK YSLKAVEDML ETLQ

UniProtKB: ER membrane protein complex subunit 2

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Macromolecule #3: ER membrane protein complex subunit 3

MacromoleculeName: ER membrane protein complex subunit 3 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.722598 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: PELLLDSNIR LWVVLPIVII TFFVGMIRHY VSILLQSDKK LTQEQVSDSQ VLIRSRVLRE NGKYIPKQSF LTRKYYFNNP EDGFFKKTK RKVVPPSPMT DPTMLTDMMK GNVTNVLPMI LIGGWINMTF SGFVTTKVPF PLTLRFKPML QQGIELLTLD A SWVSSASW ...String:
PELLLDSNIR LWVVLPIVII TFFVGMIRHY VSILLQSDKK LTQEQVSDSQ VLIRSRVLRE NGKYIPKQSF LTRKYYFNNP EDGFFKKTK RKVVPPSPMT DPTMLTDMMK GNVTNVLPMI LIGGWINMTF SGFVTTKVPF PLTLRFKPML QQGIELLTLD A SWVSSASW YFLNVFGLRS IYSLILGQDN AADQSRMMQE QMTGAAMAMP ADTNKAFKTE WEALELTDHQ WALDDVEEEL MA KDLHFEG MFKKELQTSI F

UniProtKB: ER membrane protein complex subunit 3

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Macromolecule #4: ER membrane protein complex subunit 5

MacromoleculeName: ER membrane protein complex subunit 5 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.425147 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
PSLWKGLVGI GLFALAHAAF SAAQHRSYMR LTEKEDESLP IDIVLQTLLA FAVTCYGIVH IAGEFKDMDA TSELKNKTFD TLRNHPSFY VFNHRGRVLF RP

UniProtKB: ER membrane protein complex subunit 5

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Macromolecule #5: ER membrane protein complex subunit 6

MacromoleculeName: ER membrane protein complex subunit 6 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.014019 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
PPFISEAAVR GNAAVLDYCR TSVSALSGAT AGILGLTGLY GFIFYLLASV LLSLLLILKA GRRWNKYFKS RRPLFTGGLI GGLFTYVLF WTFLYGMVHV Y

UniProtKB: ER membrane protein complex subunit 6

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Macromolecule #6: ER membrane protein complex subunit 7

MacromoleculeName: ER membrane protein complex subunit 7 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.151044 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
DRFKIEGRAV VPGVKPQDWI SAARVLVDGE EHVGFLKTDG SFVVHDIPSG SYVVEVVSPA YRFDPVRVDI TSKGKMRARY VNYIKTSEV VRLPYPLQMK SSGPPSYFIK RESWGWT

UniProtKB: Endoplasmic reticulum membrane protein complex subunit 7

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Macromolecule #7: ER membrane protein complex subunit 8

MacromoleculeName: ER membrane protein complex subunit 8 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 23.578764 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: GVKLTTQAYC KMVLHGAKYP HCAVNGLLVA EKQKPRKEHL PLGGPGAHHT LFVDCIPLFH GTLALAPMLE VALTLIDSWC KDHSYVIAG YYQANERVKD ASPNQVAEKV ASRIAEGFSD TALIMVDNTK FTMDCVAPTI HVYEHHENRW RCRDPHHDYC E DWPEAQRI ...String:
GVKLTTQAYC KMVLHGAKYP HCAVNGLLVA EKQKPRKEHL PLGGPGAHHT LFVDCIPLFH GTLALAPMLE VALTLIDSWC KDHSYVIAG YYQANERVKD ASPNQVAEKV ASRIAEGFSD TALIMVDNTK FTMDCVAPTI HVYEHHENRW RCRDPHHDYC E DWPEAQRI SASLLDSRSY ETLVDFDNHL DDIRNDWTNP EINKAVLHLC

UniProtKB: ER membrane protein complex subunit 8

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Macromolecule #8: ER membrane protein complex subunit 10

MacromoleculeName: ER membrane protein complex subunit 10 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 17.003912 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
GTVGLLLEHS FEIDDSANFR KRGSLLWNQQ DGTLSLSQRQ LSEEERGRLR DVAALNGLYR VRIPRRPGAL DGLEAGGYVS SFVPACSLV ESHLSDQLTL HVDVAGNVVG VSVVTHPGGC RGHEVEDVDL ELFNTSVQLQ PPTTAPGPET AAFIERLE

UniProtKB: ER membrane protein complex subunit 10

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Macromolecule #9: Voltage-dependent L-type calcium channel subunit alpha-1C

MacromoleculeName: Voltage-dependent L-type calcium channel subunit alpha-1C
type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 176.678766 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: LKNPIRRACI SIVEWKPFEI IILLTIFANC VALAIYIPFP EDDSNATNSN LERVEYLFLI IFTVEAFLKV IAYGLLFHPN AYLRNGWNL LDFIIVVVGL FSAILEQATK ADGANALGGK GAGFDVKALR AFRVLRPLRL VSGVPSLQVV LNSIIKAMVP L LHIALLVL ...String:
LKNPIRRACI SIVEWKPFEI IILLTIFANC VALAIYIPFP EDDSNATNSN LERVEYLFLI IFTVEAFLKV IAYGLLFHPN AYLRNGWNL LDFIIVVVGL FSAILEQATK ADGANALGGK GAGFDVKALR AFRVLRPLRL VSGVPSLQVV LNSIIKAMVP L LHIALLVL FVIIIYAIIG LELFMGKMHK TCYNQEGIAD VPAEDDPSPC ALETGHGRQC QNGTVCKPGW DGPKHGITNF DN FAFAMLT VFQCITMEGW TDVLYWVNDA VGRDWPWIYF VTLIIIGSFF VLNLVLGVLS GEFSKEREKA KARGDFQKLR EKQ QLEEDL KGYLDWITQA EDIDPENEDE GMDEEKPRNM SMPTSETESV NTENVAGGDI EGENCGARLA HRISKSKFSR YWRR WNRFC RRKCRAAVKS NVFYWLVIFL VFLNTLTIAS EHYNQPNWLT EVQDTANKAL LALFTAEMLL KMYSLGLQAY FVSLF NRFD CFVVCGGILE TILVETKIMS PLGISVLRCV RLLRIFKITR YWNSLSNLVA SLLNSVRSIA SLLLLLFLFI IIFSLL GMQ LFGGKFNFDE MQTRRSTFDN FPQSLLTVFQ ILTGEDWNSV MYDGIMAYGG PSFPGMLVCI YFIILFICGN YILLNVF LA IAVDNLADAE SLTSAQKEEE EEKERKKLAR TASPEKKQEL VEKPAVGESK EEKIELKSIT ADGESPPATK INMDDLQP N ENEDKSPYPN PETTGEEDEE EPEMPVGPRP RPLSELHLKE KAVPMPEASA FFIFSSNNRF RLQCHRIVND TIFTNLILF FILLSSISLA AEDPVQHTSF RNHILFYFDI VFTTIFTIEI ALKILGNADY VFTSIFTLEI ILKMTAYGAF LHKGSFCRNY FNILDLLVV SVSLISFGIQ SSAINVVKIL RVLRVLRPLR AINRAKGLKH VVQCVFVAIR TIGNIVIVTT LLQFMFACIG V QLFKGKLY TCSDSSKQTE AECKGNYITY KDGEVDHPII QPRSWENSKF DFDNVLAAMM ALFTVSTFEG WPELLYRSID SH TEDKGPI YNYRVEISIF FIIYIIIIAF FMMNIFVGFV IVTFQEQGEQ EYKNCELDKN QRQCVEYALK ARPLRRYIPK NQH QYKVWY VVNSTYFEYL MFVLILLNTI CLAMQHYGQS CLFKIAMNIL NMLFTGLFTV EMILKLIAFK PKGYFSDPWN VFDF LIVIG SIIDVILSET NHYFCDAWNT FDALIVVGSI VDIAITEVNP AEHTQCSPSM NAEENSRISI TFFRLFRVMR LVKLL SRGE GIRTLLWTFI KSFQALPYVA LLIVMLFFIY AVIGMQVFGK IALNDTTEIN RNNNFQTFPQ AVLLLFRCAT GEAWQD IML ACMPGKKCAP ESEPSNSTEG ETPCGSSFAV FYFISFYMLC AFLIINLFVA VIMDNFDYLT RDWSILGPHH LDEFKRI WA EYDPEAKGRI KHLDVVTLLR RIQPPLGFGK LCPHRVACKR LVSMNMPLNS DGTVMFNATL FALVRTALRI KTEGNLEQ A NEELRAIIKK IWKRTSMKLL DQVVPPAGD

UniProtKB: Voltage-dependent L-type calcium channel subunit alpha-1C

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Macromolecule #10: Voltage-dependent L-type calcium channel subunit beta-3

MacromoleculeName: Voltage-dependent L-type calcium channel subunit beta-3
type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Oryctolagus cuniculus (rabbit)
Molecular weightTheoretical: 36.692055 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: ESARREVESQ AQQQLERAKH KPVAFAVRTN VSYCGVLDEE CPVQGSGINF EAKDFLHIKE KYSNDWWIGR LVKEGGDIAF IPSPQRLES IRLKQEQKAR RSGNPSSLSD IGNRRSPPPS LAKQKQKQAE HVPPYDVVPS MRPVVLVGPS LKGYEVTDMM Q KALFDFLK ...String:
ESARREVESQ AQQQLERAKH KPVAFAVRTN VSYCGVLDEE CPVQGSGINF EAKDFLHIKE KYSNDWWIGR LVKEGGDIAF IPSPQRLES IRLKQEQKAR RSGNPSSLSD IGNRRSPPPS LAKQKQKQAE HVPPYDVVPS MRPVVLVGPS LKGYEVTDMM Q KALFDFLK HRFDGRISIT RVTADLSLAK RSVLNNPGKR TIIERSSARS SIAEVQSEIE RIFELAKSLQ LVVLDADTIN HP AQLAKTS LAPIIVFVKV SSPKVLQRLI RSRGKSQMKH LTVQMMAYDK LVQCPPESFD VILDENQLED ACEHLAEYLE VYW RATH

UniProtKB: Voltage-dependent L-type calcium channel subunit beta-3

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Macromolecule #11: ER membrane protein complex subunit 4

MacromoleculeName: ER membrane protein complex subunit 4 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 18.790051 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
RFKWAIELSG PGGGSRGRSD RGSGQGDSLY PVGYLDKQVP DTSVQETDRI LVEKRCWDIA LGPLKQIPMN LFIMYMAGNT ISIFPTMMV CMMAWRPIQA LMAISATFKM LESSSQKFLQ GLVYLIGNLM GLALAVYKCQ SMGLLPTHAS DWLAFIEPPE R MEFSGGGL LL

UniProtKB: ER membrane protein complex subunit 4

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Macromolecule #13: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 13 / Number of copies: 1 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

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Macromolecule #14: (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]sp...

MacromoleculeName: (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en
type: ligand / ID: 14 / Number of copies: 1 / Formula: 9Z9
Molecular weightTheoretical: 544.805 Da
Chemical component information

ChemComp-9Z9:
(3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en / detergent*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

Concentration1.7 mg/mL
BufferpH: 8
GridModel: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 1.7 µm / Nominal defocus min: 0.9 µm / Nominal magnification: 105000
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 46.0 e/Å2
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:

6ww7


Details: 6WW7 (PDB ID) and 7MIY (PDB ID) used to generate the startup model.
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 487067

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