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- EMDB-46054: Cryo-EM structure of MRV virion -

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Basic information

Entry
Database: EMDB / ID: EMD-46054
TitleCryo-EM structure of MRV virion
Map datamap of MRV virion
Sample
  • Virus: Mammalian orthoreovirus 3 Dearing
    • Protein or peptide: Inner capsid protein sigma-2
    • Protein or peptide: Outer capsid protein mu-1
    • Protein or peptide: Outer capsid protein sigma-3
    • Protein or peptide: Outer capsid protein lambda-2
    • Protein or peptide: Lambda 1
    • Protein or peptide: Mu2
    • Protein or peptide: RNA-directed RNA polymerase
KeywordsMammalian reovirus / outer shell / VIRAL PROTEIN
Function / homology
Function and homology information


icosahedral viral capsid / host cell surface binding / viral inner capsid / symbiont-mediated suppression of host PKR/eIFalpha signaling / host cytoskeleton / viral outer capsid / symbiont entry into host cell via permeabilization of host membrane / protein serine/threonine kinase inhibitor activity / host cell endoplasmic reticulum / 7-methylguanosine mRNA capping ...icosahedral viral capsid / host cell surface binding / viral inner capsid / symbiont-mediated suppression of host PKR/eIFalpha signaling / host cytoskeleton / viral outer capsid / symbiont entry into host cell via permeabilization of host membrane / protein serine/threonine kinase inhibitor activity / host cell endoplasmic reticulum / 7-methylguanosine mRNA capping / host cell mitochondrion / viral life cycle / viral genome replication / viral capsid / regulation of translation / mRNA guanylyltransferase activity / viral nucleocapsid / mRNA guanylyltransferase / mRNA (guanine-N7)-methyltransferase / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / host cell cytoplasm / hydrolase activity / RNA helicase activity / RNA helicase / symbiont-mediated suppression of host innate immune response / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / RNA-directed RNA polymerase / RNA-directed RNA polymerase activity / GTP binding / host cell nucleus / host cell plasma membrane / structural molecule activity / RNA binding / zinc ion binding / ATP binding / membrane
Similarity search - Function
Mu1 membrane penetration protein, domain I / Reovirus, outer capsid sigma 3 / Reovirus, outer capsid sigma-3 domain superfamily / Reovirus outer capsid protein, Sigma 3 / Outer capsid protein Mu1/VP4 / Mu1 membrane penetration protein, domain IV / Mu1 membrane penetration protein, domain II / Mu1/VP4 superfamily / Mu1 membrane penetration protein, domain III / Reovirus major virion structural protein Mu-1/Mu-1C (M2) ...Mu1 membrane penetration protein, domain I / Reovirus, outer capsid sigma 3 / Reovirus, outer capsid sigma-3 domain superfamily / Reovirus outer capsid protein, Sigma 3 / Outer capsid protein Mu1/VP4 / Mu1 membrane penetration protein, domain IV / Mu1 membrane penetration protein, domain II / Mu1/VP4 superfamily / Mu1 membrane penetration protein, domain III / Reovirus major virion structural protein Mu-1/Mu-1C (M2) / Sigma1/sigma2, reoviral / Reoviral Sigma1/Sigma2 family / Reovirus minor core protein, Mu-2 / Reovirus minor core protein Mu-2 / : / : / : / : / : / : / : / : / Reovirus core-spike protein lambda-2 (L2), 6th domain / Reovirus core-spike protein lambda-2 (L2), 7th domain / Reovirus core-spike protein lambda-2 (L2), ferredoxin-like domain / Reovirus core-spike protein lambda-2 (L2), GTase domain / Reovirus core-spike protein lambda-2 (L2), N-terminal / Reovirus core-spike protein lambda-2 (L2), methyltransferase-1 / Reovirus core-spike protein lambda-2 (L2), methyltransferase-2 / Reovirus RNA-dependent RNA polymerase lambda 3 / Reovirus RNA-dependent RNA polymerase lambda 3 / : / Inner capsid protein lambda-1/VP3 / Reovirus core-spike lambda-2 / Reovirus core-spike protein lambda-2 (L2), C-terminal / Inner capsid protein lambda-1/ VP3 / RNA-directed RNA polymerase, reovirus / RdRp of Reoviridae dsRNA viruses catalytic domain profile. / Zinc finger C2H2 type domain signature. / Zinc finger C2H2-type / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Immunoglobulin-like fold / DNA/RNA polymerase superfamily
Similarity search - Domain/homology
RNA-directed RNA polymerase / RNA helicase / Inner capsid protein sigma-2 / Outer capsid protein sigma-3 / Outer capsid protein mu-1 / Outer capsid protein lambda-2 / Mu2
Similarity search - Component
Biological speciesMammalian orthoreovirus 3 Dearing
Methodsingle particle reconstruction / cryo EM / Resolution: 3.0 Å
AuthorsLiu XY / Xia X / Martynowycz MW / Gonen T / Zhou ZH
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI094386 United States
CitationJournal: Nat Commun / Year: 2024
Title: Molecular sociology of virus-induced cellular condensates supporting reovirus assembly and replication.
Authors: Xiaoyu Liu / Xian Xia / Michael W Martynowycz / Tamir Gonen / Z Hong Zhou /
Abstract: Virus-induced cellular condensates, or viral factories, are poorly understood high-density phases where replication of many viruses occurs. Here, by cryogenic electron tomography (cryoET) of focused ...Virus-induced cellular condensates, or viral factories, are poorly understood high-density phases where replication of many viruses occurs. Here, by cryogenic electron tomography (cryoET) of focused ion beam (FIB) milling-produced lamellae of mammalian reovirus (MRV)-infected cells, we visualized the molecular organization and interplay (i.e., "molecular sociology") of host and virus in 3D at two time points post-infection, enabling a detailed description of these condensates and a mechanistic understanding of MRV replication within them. Expanding over time, the condensate fashions host ribosomes at its periphery, and host microtubules, lipid membranes, and viral molecules in its interior, forming a 3D architecture that supports the dynamic processes of viral genome replication and capsid assembly. A total of six MRV assembly intermediates are identified inside the condensate: star core, empty and genome-containing cores, empty and full virions, and outer shell particle. Except for star core, these intermediates are visualized at atomic resolution by cryogenic electron microscopy (cryoEM) of cellular extracts. The temporal sequence and spatial rearrangement among these viral intermediates choreograph the viral life cycle within the condensates. Together, the molecular sociology of MRV-induced cellular condensate highlights the functional advantage of transient enrichment of molecules at the right location and time for viral replication.
History
DepositionAug 3, 2024-
Header (metadata) releaseDec 18, 2024-
Map releaseDec 18, 2024-
UpdateDec 18, 2024-
Current statusDec 18, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_46054.png

Downloads & links

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Map

FileDownload / File: emd_46054.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationmap of MRV virion
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.1 Å/pix.
x 384 pix.
= 422.4 Å		1.1 Å/pix.
x 384 pix.
= 422.4 Å		1.1 Å/pix.
x 384 pix.
= 422.4 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.1 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.01
Minimum - Maximum-0.02446898 - 0.047663625
Average (Standard dev.)0.0007598341 (±0.004009199)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions384384384
Spacing384384384
CellA=B=C: 422.40002 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: half1 map of MRV virion

Fileemd_46054_half_map_1.map
Annotationhalf1 map of MRV virion
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half2 map of MRV virion

Fileemd_46054_half_map_2.map
Annotationhalf2 map of MRV virion
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Mammalian orthoreovirus 3 Dearing

EntireName: Mammalian orthoreovirus 3 Dearing
Components
  • Virus: Mammalian orthoreovirus 3 Dearing
    • Protein or peptide: Inner capsid protein sigma-2
    • Protein or peptide: Outer capsid protein mu-1
    • Protein or peptide: Outer capsid protein sigma-3
    • Protein or peptide: Outer capsid protein lambda-2
    • Protein or peptide: Lambda 1
    • Protein or peptide: Mu2
    • Protein or peptide: RNA-directed RNA polymerase

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Supramolecule #1: Mammalian orthoreovirus 3 Dearing

SupramoleculeName: Mammalian orthoreovirus 3 Dearing / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 10886 / Sci species name: Mammalian orthoreovirus 3 Dearing / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No
Host (natural)Organism: LLC-MK2

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Macromolecule #1: Inner capsid protein sigma-2

MacromoleculeName: Inner capsid protein sigma-2 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Mammalian orthoreovirus 3 Dearing
Molecular weightTheoretical: 47.20625 KDa
SequenceString: MARAAFLFKT VGFGGLQNVP INDELSSHLL RAGNSPWQLT QFLDWISLGR GLATSALVPT AGSRYYQMSC LLSGTLQIPF RPNHRWGDI RFLRLVWSAP TLDGLVVAPP QVLAQPALQA QADRVYDCDD YPFLARDPRF KHRVYQQLSA VTLLNLTGFG P ISYVRVDE ...String:
MARAAFLFKT VGFGGLQNVP INDELSSHLL RAGNSPWQLT QFLDWISLGR GLATSALVPT AGSRYYQMSC LLSGTLQIPF RPNHRWGDI RFLRLVWSAP TLDGLVVAPP QVLAQPALQA QADRVYDCDD YPFLARDPRF KHRVYQQLSA VTLLNLTGFG P ISYVRVDE DMWSGDVNQL LMNYFGHTFA EIAYTLCQAS ANRPWEYDGT YARMTQIVLS LFWLSYVGVI HQQNTYRTFY FQ CNRRGDA AEVWILSCSL NHSAQIRPGN RSLFVMPTSP DWNMDVNLIL SSTLTGCLCS GSQLPLIDNN SVPAVSRNIH GWT GRAGNQ LHGFQVRRMV TEFCDRLRRD GVMTQAQQNQ VEALADQTQQ FKRDKLETWA REDDQYNQAH PNSTMFRTKP FTNA QWGRG NTGATSAAIA ALI

UniProtKB: Inner capsid protein sigma-2

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Macromolecule #2: Outer capsid protein mu-1

MacromoleculeName: Outer capsid protein mu-1 / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Mammalian orthoreovirus 3 Dearing
Molecular weightTheoretical: 76.334273 KDa
SequenceString: MGNASSIVQT INVTGDGNVF KPSAETSSTA VPSLSLSPGM LNPGGVPWIA VGDETSVTSP GALRRMTSKD IPETAIINTD NSSGAVPSE SALVPYIDEP LVVVTEHAIT NFTKAEMALE FNREFLDKMR VLSVSPKYSD LLTYVDCYVG VSARQALNNF Q KQVPVITP ...String:
MGNASSIVQT INVTGDGNVF KPSAETSSTA VPSLSLSPGM LNPGGVPWIA VGDETSVTSP GALRRMTSKD IPETAIINTD NSSGAVPSE SALVPYIDEP LVVVTEHAIT NFTKAEMALE FNREFLDKMR VLSVSPKYSD LLTYVDCYVG VSARQALNNF Q KQVPVITP TRQTMYVDSI QAALKALEKW EIDLRVAQTL LPTNVPIGEV SCPMQSVVKL LDDQLPDDSL IRRYPKEAAV AL AKRNGGI QWMDVSEGTV MNEAVNAVAA SALAPSASAP PLEEKSKLTE QAMDLVTAAE PEIIASLAPV PAPVFAIPPK PAD YNVRTL RIDEATWLRM IPKSMNTPFQ IQVTDNTGTN WHLNLRGGTR VVNLDQIAPM RFVLDLGGKS YKETSWDPNG KKVG FIVFQ SKIPFELWTA ASQIGQATVV NYVQLYAEDS SFTAQSIIAT TSLAYNYEPE QLNKTDPEMN YYLLATFIDS AAITP TNMT QPDVWDALLT MSPLSAGEVT VKGAVVSEVV PADLIGSYTP ESLNASLPND AARCMIDRAS KIAEAIKIDD DAGPDE YSP NSVPIQGQLA ISQLETGYGV RIFNPKGILS KIASRAMQAF IGDPSTIITQ AAPVLSDKNN WIALAQGVKT SLRTKSL SA GVKTAVSKLS SSESIQNWTQ GFLDKVSAHF PAPKPDCPTS GDSGESSNRR VKRDSYAGVV KRGYTR

UniProtKB: Outer capsid protein mu-1

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Macromolecule #3: Outer capsid protein sigma-3

MacromoleculeName: Outer capsid protein sigma-3 / type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Mammalian orthoreovirus 3 Dearing
Molecular weightTheoretical: 41.168121 KDa
SequenceString: MEVCLPNGHQ VVDLINNAFE GRVSIYSAQE GWDKTISAQP DMMVCGGAVV CMHCLGVVGS LQRKLKHLPH HRCNQQIRHQ DYVDVQFAD RVTAHWKRGM LSFVAQMHEM MNDVSPDDLD RVRTEGGSLV ELNWLQVDPN SMFRSIHSSW TDPLQVVDDL D TKLDQYWT ...String:
MEVCLPNGHQ VVDLINNAFE GRVSIYSAQE GWDKTISAQP DMMVCGGAVV CMHCLGVVGS LQRKLKHLPH HRCNQQIRHQ DYVDVQFAD RVTAHWKRGM LSFVAQMHEM MNDVSPDDLD RVRTEGGSLV ELNWLQVDPN SMFRSIHSSW TDPLQVVDDL D TKLDQYWT ALNLMIDSSD LIPNFMMRDP SHAFNGVKLG GDARQTQFSR TFDSRSSLEW GVMVYDYSEL EHDPSKGRAY RK ELVTPAR DFGHFGLSHY SRATTPILGK MPAVFSGMLT GNCKMYPFIK GTAKLKTVRK LVEAVNHAWG VEKIRYALGP GGM TGWYNR TMQQAPIVLT PAALTMFPDT IKFGDLNYPV MIGDPMILG

UniProtKB: Outer capsid protein sigma-3

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Macromolecule #4: Outer capsid protein lambda-2

MacromoleculeName: Outer capsid protein lambda-2 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO / EC number: mRNA guanylyltransferase
Source (natural)Organism: Mammalian orthoreovirus 3 Dearing
Molecular weightTheoretical: 144.098766 KDa
SequenceString: MANVWGVRLA DSLSSPTIET RTRQYTLHDL CSDLDANPGR EPWKPLRNQR TNNIVAVQLF RPLQGLVLDT QLYGFPGAFD DWERFMREK LRVLKYEVLR IYPISNYSNE HVNVFVANAL VGAFLSNQAF YDLLPLLIIN DTMIGDLLGT GASLSQFFQS H GDVLEVAA ...String:
MANVWGVRLA DSLSSPTIET RTRQYTLHDL CSDLDANPGR EPWKPLRNQR TNNIVAVQLF RPLQGLVLDT QLYGFPGAFD DWERFMREK LRVLKYEVLR IYPISNYSNE HVNVFVANAL VGAFLSNQAF YDLLPLLIIN DTMIGDLLGT GASLSQFFQS H GDVLEVAA GRKYLQMENY SNDDDDPPLF AKDLSDYAKA FYSDTYEVLD RFFWTHDSSA GVLVHYDKPT NGHHYLLGTL TQ MVSAPPY IINATDAMLL ESCLEQFSAN VRARPAQPVT RLDQCYHLRW GAQYVGEDSL TYRLGVLSLL ATNGYQLARP IPR QLTNRW LSSFVSQIMS DGVNETPLWP QERYVQIAYD SPSVVDGATQ YGYVRKNQLR LGMRISALQS LSDTPSPVQW LPQY TIDQA AMDEGDLMVS RLTQLPLRPD YGNIWVGDAL SYYVDYNRSH RVVLSSELPQ LPDTYFDGDE QYGRSLFSLA RKIGD RSLV KDTAVLKHAY QAIDPNTGKE YLRSRQSVAY FGASAGHSGA DQPLVIEPWI QGKISGVPPP SSVRQFGYDV ARGAIV DLA RPFPSGDYQF VYSDVDQVVD GHDDLSISSG LVESLLSSCM HATAPGGSFV VKINFPTRPV WHYIEQKILP NITSYML IK PFVTNNVELF FVAFGVHQHS SLTWTSGVYF FLVDHFYRYE TLSTISRQLP SFGYVDDGSS VTGIETISIE NPGFSNMT Q AARIGISGLC ANVGNARKSI AIYESHGARV LTITSRRSPA SARRKSRLRY LPLIDPRSLE VQARTILPAD PVLFENVSG ASPHVCLTMM YNFEVSSAVY DGDVVLDLGT GPEAKILELI PATSPVTCVD IRPTAQPSGC WNVRTTFLEL DYLSDGWITG VRGDIVTCM LSLGAAAAGK SMTFDAAFQQ LIKVLSKSTA NVVLVQVNCP TDVVRSIKGY LEIDSTNKRY RFPKFGRDEP Y SDMDALEK ICRTAWPNCS ITWVPLSYDL RWTRLALLES TTLSSASIRI AELMYKYMPI MRIDIHGLPM EKRGNFIVGQ NC SLVIPGF NAQDVFNCYF NSALAFSTED VNAAMIPQVS AQFDATKGEW TLDMVFSDAG IYTMQALVGS NANPVSLGSF VVD SPDVDI TDAWPAQLDF TIAGTDVDIT VNPYYRLMTF VRIDGQWQIA NPDKFQFFSS ASGTLVMNVK LDIADKYLLY YIRD VQSRD VGFYIQHPLQ LLNTITLPTN EDLFLSAPDM REWAVKESGN TICILNSQGF VLPQDWDVLT DTISWSPSIP TYIVP PGDY TLTPL

UniProtKB: Outer capsid protein lambda-2

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Macromolecule #5: Lambda 1

MacromoleculeName: Lambda 1 / type: protein_or_peptide / ID: 5 / Number of copies: 15 / Enantiomer: LEVO
Source (natural)Organism: Mammalian orthoreovirus 3 Dearing
Molecular weightTheoretical: 141.937375 KDa
SequenceString: MKRIPRKTKG KSSGKGNDST ERADDGSSQL RDKQNNKAGP ATTEPGTSNR EQYKARPGIA SVQRATESAE MPMKNNDEGT PDKKGNTKG DLVNEHSEAK DEADEATKKQ AKDTDKSKAQ VTYSDTGINN ANELSRSGNV DNEGGSNQKP MSTRIAEATS A IVSKHPAR ...String:
MKRIPRKTKG KSSGKGNDST ERADDGSSQL RDKQNNKAGP ATTEPGTSNR EQYKARPGIA SVQRATESAE MPMKNNDEGT PDKKGNTKG DLVNEHSEAK DEADEATKKQ AKDTDKSKAQ VTYSDTGINN ANELSRSGNV DNEGGSNQKP MSTRIAEATS A IVSKHPAR VGLPPTASSG HGYQCHVCSA VLFSPLDLDA HVASHGLHGN MTLTSSDIQR HITEFISSWQ NHPIVQVSAD VE NKKTAQL LHADTPRLVT WDAGLCTSFK IVPIVPAQVP QDVLAYTFFT SSYAIQSPFP EAAVSRIVVH TRWASNVDFD RDS SVIMAP PTENNIHLFK QLLNTETLSV RGANPLMFRA NVLHMLLEFV LDNLYLNRHT GFSQDHTPFT EGANLRSLPG PDAE KWYSI MYPTRMGTPN VSKICNFVAS CVRNRVGRFD RAQMMNGAMS EWVDVFETSD ALTVSIRGRW MARLARMNIN PTEIE WALT ECAQGYVTVT SPYAPSVNRL MPYRISNAER QISQIIRIMN IGNNATVIQP VLQDISVLLQ RISPLQIDPT IISNTM STV SESTTQTLSP ASSILGKLRP SNSDFSSFRV ALAGWLYNGV VTTVIDDSSY PKDGGSVTSL ENLWDFFILA LALPLTT DP CAPVKAFMTL ANMMVGFETI PMDNQIYTQS RRASAFSTPH TWPRCFMNIQ LISPIDAPIL RQWAEIIHRY WPNPSQIR Y GAPNVFGSAN LFTPPEVLLL PIDHQPANVT TPTLDFTNEL TNWRARVCEL MKNLVDNQRY QPGWTQSLVS SMRGTLDKL KLIKSMTPMY LQQLAPVELA VIAPMLPFPP FQVPYVRLDR DRVPTMVGVT RQSRDTITQP ALSLSTTNTT VGVPLALDAR AITVALLSG KYPPDLVTNV WYADAIYPMY ADTEVFSNLQ RDMITCEAVQ TLVTLVAQIS ETQYPVDRYL DWIPSLRASA A TAATFAEW VNTSMKTAFD LSDMLLEPLL SGDPRMTQLA IQYQQYNGRT FNIIPEMPGS VIADCVQLTA EVFNHEYNLF GI ARGDIII GRVQSTHLWS PLAPPPDLVF DRDTPGVHIF GRDCRISFGM NGAAPMIRDE TGLMVPFEGN WIFPLALWQM NTR YFNQQF DAWIKTGELR IRIEMGAYPY MLHYYDPRQY ANAWNLTSAW LEEITPTSIP SVPFMVPISS DHDISSAPAV QYII STEYN DRSLFCTNSS SPQTIAGPDK HIPVERYNIL TNPDAPPTQI QLPEVVDLYN VVTRYAYETP PITAVVMGVP

UniProtKB: RNA helicase

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Macromolecule #6: Mu2

MacromoleculeName: Mu2 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mammalian orthoreovirus 3 Dearing
Molecular weightTheoretical: 83.331289 KDa
SequenceString: MAYIAVPAVV DSRSSEAIGL LESFGVDAGA DANDVSYQDH DYVLDQLQYM LDGYEAGDVI DALVHKNWLH HSVYCLLPPK SQLLEYWKS NPSAIPDNVD RRLRKRLMLK KDLRKDDEYN QLARAFKISD VYAPLISSTT SPMTMIQNLN QGEIVYTTTD R VIGARILL ...String:
MAYIAVPAVV DSRSSEAIGL LESFGVDAGA DANDVSYQDH DYVLDQLQYM LDGYEAGDVI DALVHKNWLH HSVYCLLPPK SQLLEYWKS NPSAIPDNVD RRLRKRLMLK KDLRKDDEYN QLARAFKISD VYAPLISSTT SPMTMIQNLN QGEIVYTTTD R VIGARILL YAPRKYYAST LSFTMTKCII PFGKEVGRVP HSRFNVGTFP SIATPKCFVM SGVDIESIPN EFIKLFYQRV KS VHANILN DISPQIVSDM INRKRLRVHT PSDRRAAQLM HLPYHVKRGA SHVDVYKVDV VDMLFEVVDV ADGLRNVSRK LTM HTVPVC ILEMLGIEIA DYCIRQEDGM LTDWFLLLTM LSDGLTDRRT HCQYLINPSS VPPDVILNIS ITGFINRHTI DVMP DIYDF VKPIGAVLPK GSFKSTIMRV LDSISILGIQ IMPRAHVVDS DEVGEQMEPT FEQAVMEIYK GIAGVDSLDD LIKWV LNSD LIPHDDRLGQ LFQAFLPLAK DLLAPMARKF YDNSMSEGRL LTFAHADSEL LNANYFGHLL RLKIPYITEV NLMIRK NRE GGELFQLVLS YLYKMYATSA QPKWFGSLLR LLICPWLHME KLIGEADPAS TSAEIGWHIP REQLMQDGWC GCEDGFI PY VSIRAPRLVI EELMEKNWGQ YHAQVIVTDQ LVVGEPRRVS AKAVIKGNHL PVKLVSRFAC FTLTAKYEMR LSCGHSTG R GAAYSARLAF RSDLA

UniProtKB: Mu2

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Macromolecule #7: RNA-directed RNA polymerase

MacromoleculeName: RNA-directed RNA polymerase / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO / EC number: RNA-directed RNA polymerase
Source (natural)Organism: Mammalian orthoreovirus 3 Dearing
Molecular weightTheoretical: 142.449016 KDa
SequenceString: MSSMILTQFG PFIESISGIT DQSNDVFEDA AKAFSMFTRS DVYKALDEIP FSDDAMLPIP PTIYTKPSHD SYYYIDALNR VRRKTYQGP DDVYVPNCSI VELLEPHETL TSYGRLSEAI ENRAKDGDSQ ARIATTYGRI AESQARQIKA PLEKFVLALL V AEAGGSLY ...String:
MSSMILTQFG PFIESISGIT DQSNDVFEDA AKAFSMFTRS DVYKALDEIP FSDDAMLPIP PTIYTKPSHD SYYYIDALNR VRRKTYQGP DDVYVPNCSI VELLEPHETL TSYGRLSEAI ENRAKDGDSQ ARIATTYGRI AESQARQIKA PLEKFVLALL V AEAGGSLY DPVLQKYDEI PDLSHNCPLW CFREICRHIS GPLPDRAPYL YLSAGVFWLM SPRMTSAIPP LLSDLVNLAI LQ QTAGLDP SLVKLGVQIC LHAAASSSYA WFILKTKSIF PQNTLHSMYE SLEGGYCPNL EWLEPRSDYK FMYMGVMPLS AKY ARSAPS NDKKARELGE KYGLSSVVGE LRKRTKTYVK HDFASVRYIR DAMACTSGIF LVRTPTETVL QEYTQSPEIK VPIP QKDWT GPIGEIRILK DTTSSIARYL YRTWYLAAAR MAAQPRTWDP LFQAIMRSQY VTARGGSGAA LRESLYAINV SLPDF KGLP VKAATKIFQA AQLANLPFSH TSVAILADTS MGLRNQVQRR PRSIMPLNVP QQQVSAPHTL TADYINYHMN LSTTSG SAV IEKVIPLGVY ASSPPNQSIN IDISACDASI TWDFFLSVIM AAIHEGVASS SIGKPFMGVP ASIVNDESVV GVRAARP IS GMQNMIQHLS KLYKRGFSYR VNDSFSPGND FTHMTTTFPS GSTATSTEHT ANNSTMMETF LTVWGPEHTD DPDVLRLM K SLTIQRNYVC QGDDGLMIID GTTAGKVNSE TIQKMLELIS KYGEEFGWKY DIAYDGTAEY LKLYFIFGCR IPNLSRHPI VGKERANSSA EEPWPAILDQ IMGVFFNGVH DGLQWQRWIR YSWALCCAFS RQRTMIGESV GYLQYPMWSF VYWGLPLVKA FGSDPWIFS WYMPTGDLGM YSWISLIRPL MTRWMVANGY VTDRCSPVFG NADYRRCFNE LKLYQGYYMA QLPRNPKKSG R AAPREVRE QFTQALSDYL MQNPELKSRV LRGRSEWEKY GAGIIHNPPS LFDVPHKWYQ GAQEAAIATR EELAEMDETL MR ARRHSYS SFSKLLEAYL LVKWRMCEAR EPSVDLRLPL CAGIDPLNSD PFLKMVSVGP MLQSTRKYFA QTLFMAKTVS GLD VNAIDS ALLRLRTLGA DKKALTAQLL MVGLQESEAD ALAGKIMLQD VNTVQLARVV NLAVPDTWMS LDFDSMFKHH VKLL PKDGR HLNTDIPPRM GWLRAILRFL GAGMVMTATG VAVDIYLEDI HGGGRSLGQR FMTWMRQEGR SA

UniProtKB: RNA-directed RNA polymerase

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4 / Details: Phosphate-buffered saline
GridModel: Quantifoil R2/1 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY
VitrificationCryogen name: ETHANE / Chamber humidity: 100 %

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Specialist opticsEnergy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 1 / Number real images: 22739 / Average exposure time: 2.0 sec. / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.6 µm / Nominal defocus min: 1.8 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

Particle selectionNumber selected: 592105
Startup modelType of model: EMDB MAP
EMDB ID:

31188

Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Number images used: 97187
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-9cyy:
Cryo-EM structure of MRV virion

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