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- EMDB-21861: Cryo-EM structure of recombinant mouse Ryanodine Receptor type 2 ... -

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Basic information

Entry
Database: EMDB / ID: EMD-21861
TitleCryo-EM structure of recombinant mouse Ryanodine Receptor type 2 mutant R176Q in complex with FKBP12.6 in nanodisc
Map data
Sample
  • Complex: recombinant mouse Ryanodine Receptor type 2, RyR2, with mutation R176Q in complex with FKBP12.6
    • Complex: recombinant mouse Ryanodine Receptor type 2, RyR2, with mutation R176Q
      • Protein or peptide: Ryanodine receptor 2
    • Complex: FKBP12.6
      • Protein or peptide: Peptidyl-prolyl cis-trans isomerase FKBP1B
  • Ligand: ZINC ION
KeywordsRyanodine receptor / Calcium channel / Mutation / NTDA mutation / RyR2 / Polymorphic catecholergic ventricular tachycardia / Arrhythmogenic Right Ventricular Dysplasia 2 / TRANSPORT PROTEIN-ISOMERASE complex
Function / homology
Function and homology information


manganese ion transmembrane transport / establishment of protein localization to endoplasmic reticulum / type B pancreatic cell apoptotic process / Purkinje myocyte to ventricular cardiac muscle cell signaling / suramin binding / regulation of SA node cell action potential / regulation of atrial cardiac muscle cell action potential / left ventricular cardiac muscle tissue morphogenesis / organic cyclic compound binding / regulation of AV node cell action potential ...manganese ion transmembrane transport / establishment of protein localization to endoplasmic reticulum / type B pancreatic cell apoptotic process / Purkinje myocyte to ventricular cardiac muscle cell signaling / suramin binding / regulation of SA node cell action potential / regulation of atrial cardiac muscle cell action potential / left ventricular cardiac muscle tissue morphogenesis / organic cyclic compound binding / regulation of AV node cell action potential / calcium-induced calcium release activity / sarcoplasmic reticulum calcium ion transport / Stimuli-sensing channels / Ion homeostasis / regulation of ventricular cardiac muscle cell action potential / ventricular cardiac muscle cell action potential / positive regulation of sequestering of calcium ion / cyclic nucleotide binding / negative regulation of calcium-mediated signaling / embryonic heart tube morphogenesis / cardiac muscle hypertrophy / negative regulation of insulin secretion involved in cellular response to glucose stimulus / calcium ion transport into cytosol / negative regulation of release of sequestered calcium ion into cytosol / neuronal action potential propagation / insulin secretion involved in cellular response to glucose stimulus / ryanodine-sensitive calcium-release channel activity / response to caffeine / response to muscle activity / A band / release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / calcium ion transmembrane import into cytosol / response to redox state / protein maturation by protein folding / 'de novo' protein folding / negative regulation of heart rate / positive regulation of heart rate / FK506 binding / negative regulation of cytosolic calcium ion concentration / positive regulation of axon regeneration / protein kinase A regulatory subunit binding / extrinsic component of cytoplasmic side of plasma membrane / cellular response to caffeine / channel regulator activity / protein kinase A catalytic subunit binding / response to magnesium ion / positive regulation of the force of heart contraction / intracellularly gated calcium channel activity / detection of calcium ion / smooth muscle contraction / response to vitamin E / smooth endoplasmic reticulum / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / calcium channel inhibitor activity / striated muscle contraction / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / T cell proliferation / Ion homeostasis / release of sequestered calcium ion into cytosol / regulation of cytosolic calcium ion concentration / calcium channel complex / cellular response to epinephrine stimulus / sarcoplasmic reticulum membrane / response to muscle stretch / regulation of heart rate / sarcomere / sarcoplasmic reticulum / establishment of localization in cell / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / calcium-mediated signaling / calcium ion transmembrane transport / response to hydrogen peroxide / calcium channel activity / Stimuli-sensing channels / sarcolemma / Z disc / response to calcium ion / intracellular calcium ion homeostasis / calcium ion transport / nuclear envelope / positive regulation of cytosolic calcium ion concentration / monoatomic ion transmembrane transport / protein refolding / scaffold protein binding / transmembrane transporter binding / response to hypoxia / calmodulin binding / signaling receptor binding / calcium ion binding / protein kinase binding / enzyme binding / protein-containing complex / identical protein binding / membrane / cytosol / cytoplasm
Similarity search - Function
Ryanodine receptor, SPRY domain 2 / : / Ryanodine receptor junctional solenoid repeat / Ryanodine Receptor TM 4-6 / Ryanodine receptor / Ryanodine receptor, SPRY domain 1 / Ryanodine receptor, SPRY domain 3 / Ryanodine Receptor TM 4-6 / Ryanodine receptor Ryr / RyR domain ...Ryanodine receptor, SPRY domain 2 / : / Ryanodine receptor junctional solenoid repeat / Ryanodine Receptor TM 4-6 / Ryanodine receptor / Ryanodine receptor, SPRY domain 1 / Ryanodine receptor, SPRY domain 3 / Ryanodine Receptor TM 4-6 / Ryanodine receptor Ryr / RyR domain / RyR/IP3 receptor binding core, RIH domain superfamily / RyR/IP3R Homology associated domain / Inositol 1,4,5-trisphosphate/ryanodine receptor / RIH domain / RyR and IP3R Homology associated / Inositol 1,4,5-trisphosphate/ryanodine receptor / : / RIH domain / : / MIR motif / MIR domain / MIR domain profile. / Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases / Mir domain superfamily / SPRY domain / B30.2/SPRY domain / B30.2/SPRY domain profile. / B30.2/SPRY domain superfamily / Domain in SPla and the RYanodine Receptor. / SPRY domain / FKBP-type peptidyl-prolyl cis-trans isomerase domain profile. / FKBP-type peptidyl-prolyl cis-trans isomerase domain / FKBP-type peptidyl-prolyl cis-trans isomerase / Peptidyl-prolyl cis-trans isomerase domain superfamily / EF-hand domain pair / EF-hand domain / Ion transport domain / Ion transport protein / EF-hand domain pair / Concanavalin A-like lectin/glucanase domain superfamily
Similarity search - Domain/homology
Ryanodine receptor 2 / Peptidyl-prolyl cis-trans isomerase FKBP1B
Similarity search - Component
Biological speciesMus musculus (house mouse) / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.27 Å
AuthorsIyer KA / Hu Y / Kurebayashi N / Murayama T / Samso M
Funding support United States, 7 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIH/NIAMS)R01 AR068431 United States
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)R01 HL133182 United States
Other privateMDA 352845 United States
American Heart Association19POST34430178 United States
National Institutes of Health/National Cancer Institute (NIH/NCI)HSSN26120080001E United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)U24 GM116789 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)U24 GM116790 United States
CitationJournal: Sci Adv / Year: 2020
Title: Structural mechanism of two gain-of-function cardiac and skeletal RyR mutations at an equivalent site by cryo-EM.
Authors: Kavita A Iyer / Yifan Hu / Ashok R Nayak / Nagomi Kurebayashi / Takashi Murayama / Montserrat Samsó /
Abstract: Mutations in ryanodine receptors (RyRs), intracellular Ca channels, are associated with deadly disorders. Despite abundant functional studies, the molecular mechanism of RyR malfunction remains ...Mutations in ryanodine receptors (RyRs), intracellular Ca channels, are associated with deadly disorders. Despite abundant functional studies, the molecular mechanism of RyR malfunction remains elusive. We studied two single-point mutations at an equivalent site in the skeletal (RyR1 R164C) and cardiac (RyR2 R176Q) isoforms using ryanodine binding, Ca imaging, and cryo-electron microscopy (cryo-EM) of the full-length protein. Loss of the positive charge had greater effect on the skeletal isoform, mediated via distortion of a salt bridge network, a molecular latch inducing rotation of a cytoplasmic domain, and partial progression to open-state traits of the large cytoplasmic assembly accompanied by alteration of the Ca binding site, which concur with the major "hyperactive" feature of the mutated channel. Our cryo-EM studies demonstrated the allosteric effect of a mutation situated ~85 Å away from the pore and identified an isoform-specific structural effect.
History
DepositionApr 25, 2020-
Header (metadata) releaseAug 5, 2020-
Map releaseAug 5, 2020-
UpdateMay 29, 2024-
Current statusMay 29, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.15
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  • Surface view colored by cylindrical radius
  • Surface level: 0.15
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  • Surface view with fitted model
  • Atomic models: PDB-6wou
  • Surface level: 0.15
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6wou
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_21861.png

Downloads & links

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Map

FileDownload / File: emd_21861.map.gz / Format: CCP4 / Size: 381.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.08 Å/pix.
x 464 pix.
= 501.12 Å		1.08 Å/pix.
x 464 pix.
= 501.12 Å		1.08 Å/pix.
x 464 pix.
= 501.12 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.08 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.132 / Movie #1: 0.15
Minimum - Maximum-0.9546881 - 1.71456
Average (Standard dev.)0.0008855611 (±0.042270444)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions464464464
Spacing464464464
CellA=B=C: 501.12003 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.081.081.08
M x/y/z464464464
origin x/y/z0.0000.0000.000
length x/y/z501.120501.120501.120
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ256256256
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS464464464
D min/max/mean-0.9551.7150.001

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Supplemental data

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Mask #1

Fileemd_21861_msk_1.map
Projections & Slices
AxesZYX

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Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_21861_half_map_1.map
Projections & Slices
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Half map: #1

Fileemd_21861_half_map_2.map
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Sample components

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Entire : recombinant mouse Ryanodine Receptor type 2, RyR2, with mutation ...

EntireName: recombinant mouse Ryanodine Receptor type 2, RyR2, with mutation R176Q in complex with FKBP12.6
Components
  • Complex: recombinant mouse Ryanodine Receptor type 2, RyR2, with mutation R176Q in complex with FKBP12.6
    • Complex: recombinant mouse Ryanodine Receptor type 2, RyR2, with mutation R176Q
      • Protein or peptide: Ryanodine receptor 2
    • Complex: FKBP12.6
      • Protein or peptide: Peptidyl-prolyl cis-trans isomerase FKBP1B
  • Ligand: ZINC ION

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Supramolecule #1: recombinant mouse Ryanodine Receptor type 2, RyR2, with mutation ...

SupramoleculeName: recombinant mouse Ryanodine Receptor type 2, RyR2, with mutation R176Q in complex with FKBP12.6
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Molecular weightTheoretical: 2.26 MDa

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Supramolecule #2: recombinant mouse Ryanodine Receptor type 2, RyR2, with mutation R176Q

SupramoleculeName: recombinant mouse Ryanodine Receptor type 2, RyR2, with mutation R176Q
type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1
Source (natural)Organism: Mus musculus (house mouse)

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Supramolecule #3: FKBP12.6

SupramoleculeName: FKBP12.6 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Ryanodine receptor 2

MacromoleculeName: Ryanodine receptor 2 / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 565.507 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MADAGEGEDE IQFLRTDDEV VLQCTATIHK EQQKLCLAAE GFGNRLCFLE STSNSKNVPP DLSICTFVLE QSLSVRALQE MLANTVEKS EGQVDVEKWK FMMKTAQGGG HRTLLYGHAI LLRHSYSGMY LCCLSTSRSS TDKLAFDVGL QEDTTGEACW W TIHPASKQ ...String:
MADAGEGEDE IQFLRTDDEV VLQCTATIHK EQQKLCLAAE GFGNRLCFLE STSNSKNVPP DLSICTFVLE QSLSVRALQE MLANTVEKS EGQVDVEKWK FMMKTAQGGG HRTLLYGHAI LLRHSYSGMY LCCLSTSRSS TDKLAFDVGL QEDTTGEACW W TIHPASKQ RSEGEKVQVG DDLILVSVSS ERYLHLSYGN SSWHVDAAFQ QTLWSVAPIS SGSEAAQGYL IGGDVLRLLH GH MDECLTV PSGEHGEEQR RTVHYEGGAV SVHARSLWRL ETLRVAWSGS HIRWGQPFRL RHVTTGKYLS LMEDKNLLLM DKE KADVKS TAFAFRSSKE KLDVGVRKEV DGMGTSEIKY GDSICYIQHV DTGLWLTYQA VDVKSARMGS IQRKAIMHHE GHMD DGLNL SRSQHEESRT ARVIRSTVFL FNRFIRGLDA LSKKVKLPTI DLPIESVSLS LQDLIGYFHP PDEHLEHEDK QNRLR ALKN RQNLFQEEGM INLVLECIDR LHVYSSAAHF ADVAGREAGE SWKSILNSLY ELLAALIRGN RKNCAQFSGS LDWLIS RLE RLEASSGILE VLHCVLVESP EALNIIKEGH IKSIISLLDK HGRNHKVLDV LCSLCVCHGV AVRSNQHLIC DNLLPGR DL LLQTRLVNHV SSMRPNIFLG VSEGSAQYKK WYYELMVDHT EPFVTAEATH LRVGWASTEG YSPYPGGGEE WGGNGVGD D LFSYGFDGLH LWSGCIARTV SSPNQHLLRT DDVISCCLDL SAPSISFRIN GQPVQGMFEN FNIDGLFFPV VSFSAGIKV RFLLGGRHGE FKFLPPPGYA ACYEAVLPKE KLKVEHSREY KQERTYTRDL LGPTVSLTQA AFTPVPVDTS QIVLPPHLER IRERLAENI HELWVMNKIE LGWQYGPVRD DNKRQHPCLV EFCKLPEQER NYNLQMSLET LKTLLALGCH VGIADEHAEE K VKKMKLPK NYQLTSGYKP APMDLSFIKL TPSQEAMVDK LAENAHNVWA RDRIRQGWTY GIQQDVKNRR NPRLVPYTLL DD RTKKSNK DSLREAVRTL LGYGYHLEAP DQDHASRAEV CSGTGERFRI FRAEKTYAVK AGRWYFEFEA VTAGDMRVGW SRP GCQPDL ELGSDDRAFA FDGFKAQRWH QGNEHYGRSW QAGDVVGCMV DMNEHTMMFT LNGEILLDDS GSELAFKDFD VGDG FIPVC SLGVAQVGRM NFGKDVSTLK YFTICGLQEG YEPFAVNTNR DITMWLSKRL PQFLQVPSNH EHIEVTRIDG TIDSS PCLK VTQKSFGSQN NNTDIMFYRL SMPIECAEVF SKSVAGGLPG AGFYGPKNDL EDFDVDSDFE VLMKTAHGHL VPDRID KDK ETPKPEFNNH KDYAQEKPSR LKQRFLLRRT KPDYSTGHSA RLTEDVLADD RDDYEYLMQT STYYYSVRIF PGQEPAN VW VGWITSDFHQ YDTGFDLDRV RTVTVTLGDE KGKVHESIKR SNCYMVCAGE SMSPGQGRNN SNGLEIGCVV DAASGLLT F IANGKELSTY YQVEPSTKLF PAVFAQATSP NVFQFELGRI KNVMPLSAGL FKSEHKNPVP QCPPRLHVQF LSHVLWSRM PNQFLKVDVS RISERQGWLV QCLDPLQFMS LHIPEENRSV DILELTEQEE LLQFHYHTLR LYSAVCALGN HRVAHALCSH VDEPQLLYA IENKYMPGLL RAGYYDLLID IHLSSYATAR LMMNNEFIVP MTEETKSITL FPDENKKHGL PGIGLSTSLR P RMRFSSPS FVSISNDCYQ YSPEFPLDIL KAKTIQMLTE AVKEGSLHAR DPVGGTTEFL FVPLIKLFYT LLIMGIFHNE DL KHILQLI EPSVFKEAAV PEEEGGTPEK EISIEDAKLE GEEEAKGGKR PKEGLLQMKL PEPVKLQMCL LLQYLCDCQV RHR IEAIVA FSDDFVAKLQ DNQRFRYNEV MQALNMSAAL TARKTREFRS PPQEQINMLL NFKDDKSECP CPEEIRDQLL DFHE DLMTH CGIELDEDGS LDGSNDLTIR GRLLSLVEKV TYLKKKQAEK PVASDSRKCS SLQQLISETM VRWAQESVIE DPELV RAMF VLLHRQYDGI GGLVRALPKT YTINGVSVED TINLLASLGQ IRSLLSVRMG KEEEKLMIRG LGDIMNNKVF YQHPNL MRA LGMHETVMEV MVNVLGGGES KEITFPKMVA NCCRFLCYFC RISRQNQKAM FDHLSYLLEN SSVGLASPAM RGSTPLD VA AASVMDNNEL ALALREPDLE KVVRYLAGCG LQSCQMLVSK GYPDIGWNPV EGERYLDFLR FAVFCNGESV EENANVVV R LLIRRPECFG PALRGEGGNG LLAAMEEAIK IAEDPSRDGP SPTSGSSKTL DIEEEEDDTI HMGNAIMTFY AALIDLLGR CAPEMHLIHA GKGEAIRIRS ILRSLIPLGD LVGVISIAFQ MPTIAKDGKV VEPDMSAGFC PDHKAAMVLF LDRVYGIEVQ DFLLHLLEV GFLPDLRAAA SLDTAALSAT DMALALNRYL CTAVLPLLTR CAPLFAGTEH HASLIDSLLH TVYRLSKGCS L TKAQRDSI EVCLLSICGQ LRPSMMQHLL RRLVFDVPLL NEHAKMPLKL LTNHYERCWK YYCLPGGWGN FGAASEEELH LS RKLFWGI FDALSQKKYE QELFKLALPC LSAVAGALPP DYMESNYVSM MEKQSSMDSE GNFNPQPVDT SNITIPEKLE YFI NKYAEH SHDKWSMDKL ANGWIYGEIY SDSSKIQPLM KPYKLLSEKE KEIYRWPIKE SLKTMLAWGW RIERTREGDS MALY NRTRR ISQTSQVSID AAHGYSPRAI DMSNVTLSRD LHAMAEMMAE NYHNIWAKKK KLELESKGGG NHPLLVPYDT LTAKE KAKD REKAQDIFKF LQISGYVVSR GFKDLDLDTP SIEKRFAYSF LQQLIRYVDE AHQYILEFDG GSRSKGEHFP YEQEIK FFA KVVLPLIDQY FKNHRLYFLS AASRPLCTGG HASNKEKEMV TSLFCKLGVL VRHRISLFGN DATSIVNCLH ILGQTLD AR TVMKTGLDSV KSALRAFLDN AAEDLEKTME NLKQGQFTHT RSQPKGVTQI INYTTVALLP MLSSLFEHIG QHQFGEDL I LEDVQVSCYR ILTSLYALGT SKSIYVERQR SALGECLAAF AGAFPIAFLE THLDKHNVYS IYNTRSSRER AALSLPANV EDVCPNIPSL EKLMTEIIEL AESGIRYTQM PYMMEVVLPM LCSYMSRWWE HGPENHPERA EMCCTALNSE HMNTLLGNIL KIIYNNLGI DEGAWMKRLA VFSQPIINKV KPQLLKTHFL PLMEKLKKKA AMVVSEEDHL KAEARGDMSE AELLILDEFT T LARDLYAF YPLLIRFVDY NRAKWLKEPN PEAEELFRMV AEVFIYWSKS HNFKREEQNF VVQNEINNMS FLITDTKSKM SK AAISDQE RKKMKRKGDR YSMQTSLIVA ALKRLLPIGL NICAPGDQEL IALAKNRFSL KDTEEEVRDI IRSNIHLQGK LED PAIRWQ MALYKDLPNR TEDPSDPERT VERVLGIANV LFHLEQKSKY TGRGYFSLVE HPQRSKKAVW HKLLSKQRKR AVVA CFRMA PLYNLPRHRA VNLFLQGYEK SWIETEEHYF EDKLIEDLAK PGAELPEEDE AMKRVDPLHQ LILLFSRTAL TEKCK LEED FLYMAYADIM AKSCHDEEDD DGEEEVKSFE EKEMEKQKLL YQQARLHDRG AAEMVLQTIS ASKGETGPMV AATLKL GIA ILNGGNSTVQ QKMLDYLKEK KDVGFFQSLA GLMQSCSVLD LNAFERQNKA EGLGMVTEEG SGEKVLQDDE FTCDLFR FL QLLCEGHNSD FQNYLRTQTG NNTTVNIIIS TVDYLLRVQE SISDFYWYYS GKDIIDEQGQ RNFSKAIQVA KQVFNTLT E YIQGPCTGNQ QSLAHSRLWD AVVGFLHVFA HMQMKLSQDS SQIELLKELM DLQKDMVVML LSMLEGNVVN GTIGKQMVD MLVESSNNVE MILKFFDMFL KLKDLTSSDT FKEYDPDGKG VISKRDFHKA MESHKHYTQS ETEFLLSCAE TDENETLDYE EFVKRFHEP AKDIGFNVAV LLTNLSEHMP NDTRLQTFLE LAESVLNYFQ PFLGRIEIMG SAKRIERVYF EISESSRTQW E KPQVKESK RQFIFDVVNE GGEKEKMELF VNFCEDTIFE MQLAAQISES DLNERLANKE ESEKERPEEQ APRMGFFSLL TI QSALFAL RYNVLTLVRM LSLKSLKKQM KRMKKMTVKD MVLAFFSSYW SVFVTLLHFV ASVCRGFFRI VSSLLLGGSL VEG AKKIKV AELLANMPDP TQDEVRGDEE EGERKPLESA LPSEDLTDLK ELTEESDLLS DIFGLDLKRE GGQYKLIPHN PNAG LSDLM TNPVPVPEVQ EKFQEQKAKE EKEEKEETKS EPEKAEGEDG EKEEKAKDEK SKQKLRQLHT HRYGEPEVPE SAFWK KIIA YQQKLLNYFA RNFYNMRMLA LFVAFAINFI LLFYKVSTSS VVEGKELPTR TSSDTAKVTN SLDSSPHRII AVHYVL EES SGYMEPTLRI LAILHTIISF FCIIGYYCLK VPLVIFKREK EVARKLEFDG LYITEQPSED DIKGQWDRLV INTQSFP NN YWDKFVKRKV MDKYGEFYGR DRISELLGMD KAALDFSDAR EKKKPKKDSS LSAVLNSIDV KYQMWKLGVV FTDNSFLY L AWYMTMSVLG HYNNFFFAAH LLDIAMGFKT LRTILSSVTH NGKQLVLTVG LLAVVVYLYT VVAFNFFRKF YNKSEDGDT PDMKCDDMLT CYMFHMYVGV RAGGGIGDEI EDPAGDEYEI YRIIFDITFF FFVIVILLAI IQGLIIDAFG ELRDQQEQVK EDMETKCFI CGIGNDYFDT VPHGFETHTL QEHNLANYLF FLMYLINKDE TEHTGQESYV WKMYQERCWE FFPAGDCFRK Q YEDQLN

UniProtKB: Ryanodine receptor 2

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Macromolecule #2: Peptidyl-prolyl cis-trans isomerase FKBP1B

MacromoleculeName: Peptidyl-prolyl cis-trans isomerase FKBP1B / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO / EC number: peptidylprolyl isomerase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.667305 KDa
Recombinant expressionOrganism: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
SequenceString:
GVEIETISPG DGRTFPKKGQ TCVVHYTGML QNGKKFDSSR DRNKPFKFRI GKQEVIKGFE EGAAQMSLGQ RAKLTCTPDV AYGATGHPG VIPPNATLIF DVELLNLE

UniProtKB: Peptidyl-prolyl cis-trans isomerase FKBP1B

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Macromolecule #3: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 3 / Number of copies: 4 / 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

Concentration4.00 mg/mL
BufferpH: 7.4
Component:
ConcentrationNameFormula
20.0 mMMOPS
0.6 Mpotassium chlorideKCl
2.0 mMdithiothreitol
2.0 mMEGTA
GridModel: Quantifoil, UltrAuFoil, R1.2/1.3 / Material: GOLD / Mesh: 300
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Specialist opticsEnergy filter - Slit width: 20 eV
Image recording#0 - Image recording ID: 1 / #0 - Film or detector model: GATAN K3 (6k x 4k) / #0 - Number grids imaged: 1 / #0 - Number real images: 8655 / #0 - Average exposure time: 3.4 sec. / #0 - Average electron dose: 50.0 e/Å2 / #1 - Image recording ID: 2 / #1 - Film or detector model: GATAN K3 (6k x 4k) / #1 - Number grids imaged: 1 / #1 - Number real images: 8655 / #1 - Average exposure time: 3.4 sec. / #1 - Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 81000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Image recording ID1
Particle selectionNumber selected: 860841
Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: C4 (4 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.27 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 2.11) / Number images used: 282778
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 2.11)
Final angle assignmentType: PROJECTION MATCHING / Software - Name: cryoSPARC (ver. 2.11)

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Atomic model buiding 1

Initial modelPDB ID:

5l1d


Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-6wou:
Cryo-EM structure of recombinant mouse Ryanodine Receptor type 2 mutant R176Q in complex with FKBP12.6 in nanodisc

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