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- EMDB-23526: Human TRiC/CCT complex with reovirus outer capsid protein sigma-3 -

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Basic information

Entry
Database: EMDB / ID: EMD-23526
TitleHuman TRiC/CCT complex with reovirus outer capsid protein sigma-3
Map data
Sample
  • Complex: human TRiC/CCT complex with reovirus outer capsid protein sigma-3
    • Complex: human TRiC/CCT complex
      • Protein or peptide: x 8 types
    • Complex: reovirus outer capsid protein sigma-3
      • Protein or peptide: x 1 types
  • Ligand: x 2 types
Keywordstric / cct / reovirus capsid / sigma 3 / CHAPERONE
Function / homology
Function and homology information


symbiont-mediated suppression of host PKR/eIFalpha signaling / zona pellucida receptor complex / scaRNA localization to Cajal body / viral outer capsid / positive regulation of protein localization to Cajal body / tubulin complex assembly / chaperone mediated protein folding independent of cofactor / positive regulation of establishment of protein localization to telomere / BBSome-mediated cargo-targeting to cilium / chaperonin-containing T-complex ...symbiont-mediated suppression of host PKR/eIFalpha signaling / zona pellucida receptor complex / scaRNA localization to Cajal body / viral outer capsid / positive regulation of protein localization to Cajal body / tubulin complex assembly / chaperone mediated protein folding independent of cofactor / positive regulation of establishment of protein localization to telomere / BBSome-mediated cargo-targeting to cilium / chaperonin-containing T-complex / Folding of actin by CCT/TriC / positive regulation of telomerase RNA localization to Cajal body / Formation of tubulin folding intermediates by CCT/TriC / binding of sperm to zona pellucida / Prefoldin mediated transfer of substrate to CCT/TriC / protein serine/threonine kinase inhibitor activity / RHOBTB1 GTPase cycle / intermediate filament cytoskeleton / WD40-repeat domain binding / beta-tubulin binding / pericentriolar material / Association of TriC/CCT with target proteins during biosynthesis / chaperone-mediated protein complex assembly / heterochromatin / RHOBTB2 GTPase cycle / chaperone-mediated protein folding / protein folding chaperone / viral life cycle / positive regulation of telomerase activity / positive regulation of telomere maintenance via telomerase / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / acrosomal vesicle / mRNA 3'-UTR binding / cell projection / ATP-dependent protein folding chaperone / response to virus / mRNA 5'-UTR binding / cilium / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / G-protein beta-subunit binding / azurophil granule lumen / melanosome / unfolded protein binding / protein folding / cell body / secretory granule lumen / microtubule / ficolin-1-rich granule lumen / protein stabilization / cytoskeleton / cadherin binding / centrosome / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / ubiquitin protein ligase binding / Neutrophil degranulation / structural molecule activity / Golgi apparatus / ATP hydrolysis activity / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding / metal ion binding / cytosol / cytoplasm
Similarity search - Function
Reovirus, outer capsid sigma 3 / Reovirus, outer capsid sigma-3 domain superfamily / Reovirus outer capsid protein, Sigma 3 / T-complex protein 1, alpha subunit / T-complex protein 1, eta subunit / T-complex protein 1, theta subunit / T-complex protein 1, zeta subunit / T-complex protein 1, delta subunit / T-complex protein 1, gamma subunit / T-complex protein 1, epsilon subunit ...Reovirus, outer capsid sigma 3 / Reovirus, outer capsid sigma-3 domain superfamily / Reovirus outer capsid protein, Sigma 3 / T-complex protein 1, alpha subunit / T-complex protein 1, eta subunit / T-complex protein 1, theta subunit / T-complex protein 1, zeta subunit / T-complex protein 1, delta subunit / T-complex protein 1, gamma subunit / T-complex protein 1, epsilon subunit / T-complex protein 1, beta subunit / Chaperonins TCP-1 signature 1. / Chaperonins TCP-1 signature 2. / Chaperonin TCP-1, conserved site / Chaperonins TCP-1 signature 3. / Chaperone tailless complex polypeptide 1 (TCP-1) / GroEL-like equatorial domain superfamily / TCP-1-like chaperonin intermediate domain superfamily / GroEL-like apical domain superfamily / TCP-1/cpn60 chaperonin family / Chaperonin Cpn60/GroEL/TCP-1 family
Similarity search - Domain/homology
Outer capsid protein sigma-3 / T-complex protein 1 subunit alpha / T-complex protein 1 subunit zeta / T-complex protein 1 subunit epsilon / T-complex protein 1 subunit gamma / T-complex protein 1 subunit theta / T-complex protein 1 subunit delta / T-complex protein 1 subunit beta / T-complex protein 1 subunit eta
Similarity search - Component
Biological speciesHomo sapiens (human) / Mammalian orthoreovirus 3 Dearing / Reovirus type 3 (strain Dearing)
Methodsingle particle reconstruction / cryo EM / Resolution: 6.2 Å
AuthorsKnowlton JJ / Gestaut D / Ma B / Taylor G / Seven AB / Leitner A / Wilson GJ / Shanker S / Yates NA / Prasad BVV ...Knowlton JJ / Gestaut D / Ma B / Taylor G / Seven AB / Leitner A / Wilson GJ / Shanker S / Yates NA / Prasad BVV / Aebersold R / Chiu W / Frydman J / Dermody TS
Funding support United States, European Union, 10 items
OrganizationGrant numberCountry
Robert A. Welch FoundationQ1279 United States
National Institutes of Health/National Center for Advancing Translational Sciences (NIH/NCATS)UL1TR000445 United States
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)P41GM103832 United States
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)P01NS092525 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM007347 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM074074 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM103124 United States
National Institutes of Health/National Center for Advancing Translational Sciences (NIH/NCATS)UL1TR000445 United States
European Research Council (ERC)AdvG 233226European Union
European Research Council (ERC)AdvG 670821European Union
CitationJournal: Proc Natl Acad Sci U S A / Year: 2021
Title: Structural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC/CCT chaperone network.
Authors: Jonathan J Knowlton / Daniel Gestaut / Boxue Ma / Gwen Taylor / Alpay Burak Seven / Alexander Leitner / Gregory J Wilson / Sreejesh Shanker / Nathan A Yates / B V Venkataram Prasad / Ruedi ...Authors: Jonathan J Knowlton / Daniel Gestaut / Boxue Ma / Gwen Taylor / Alpay Burak Seven / Alexander Leitner / Gregory J Wilson / Sreejesh Shanker / Nathan A Yates / B V Venkataram Prasad / Ruedi Aebersold / Wah Chiu / Judith Frydman / Terence S Dermody /
Abstract: Intracellular protein homeostasis is maintained by a network of chaperones that function to fold proteins into their native conformation. The eukaryotic TRiC chaperonin (TCP1-ring complex, also ...Intracellular protein homeostasis is maintained by a network of chaperones that function to fold proteins into their native conformation. The eukaryotic TRiC chaperonin (TCP1-ring complex, also called CCT for cytosolic chaperonin containing TCP1) facilitates folding of a subset of proteins with folding constraints such as complex topologies. To better understand the mechanism of TRiC folding, we investigated the biogenesis of an obligate TRiC substrate, the reovirus σ3 capsid protein. We discovered that the σ3 protein interacts with a network of chaperones, including TRiC and prefoldin. Using a combination of cryoelectron microscopy, cross-linking mass spectrometry, and biochemical approaches, we establish functions for TRiC and prefoldin in folding σ3 and promoting its assembly into higher-order oligomers. These studies illuminate the molecular dynamics of σ3 folding and establish a biological function for TRiC in virus assembly. In addition, our findings provide structural and functional insight into the mechanism by which TRiC and prefoldin participate in the assembly of protein complexes.
History
DepositionFeb 22, 2021-
Header (metadata) releaseMar 3, 2021-
Map releaseMar 3, 2021-
UpdateMar 6, 2024-
Current statusMar 6, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.03
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.03
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7lup
  • Surface level: 0.03
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_23526.png

Downloads & links

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Map

FileDownload / File: emd_23526.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.3 Å
Density
Contour LevelBy AUTHOR: 0.03 / Movie #1: 0.03
Minimum - Maximum-0.047958057 - 0.11017059
Average (Standard dev.)0.0008743488 (±0.0063731084)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions280280280
Spacing280280280
CellA=B=C: 364.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.31.31.3
M x/y/z280280280
origin x/y/z0.0000.0000.000
length x/y/z364.000364.000364.000
α/β/γ90.00090.00090.000
start NX/NY/NZ645365
NX/NY/NZ139143124
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS280280280
D min/max/mean-0.0480.1100.001

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Supplemental data

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Sample components

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Entire : human TRiC/CCT complex with reovirus outer capsid protein sigma-3

EntireName: human TRiC/CCT complex with reovirus outer capsid protein sigma-3
Components
  • Complex: human TRiC/CCT complex with reovirus outer capsid protein sigma-3
    • Complex: human TRiC/CCT complex
      • Protein or peptide: T-complex protein 1 subunit epsilon
      • Protein or peptide: T-complex protein 1 subunit beta
      • Protein or peptide: T-complex protein 1 subunit delta
      • Protein or peptide: T-complex protein 1 subunit gamma
      • Protein or peptide: T-complex protein 1 subunit eta
      • Protein or peptide: T-complex protein 1 subunit theta
      • Protein or peptide: T-complex protein 1 subunit zeta
      • Protein or peptide: T-complex protein 1 subunit alpha
    • Complex: reovirus outer capsid protein sigma-3
      • Protein or peptide: Outer capsid protein sigma-3
  • Ligand: ZINC ION
  • Ligand: water

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Supramolecule #1: human TRiC/CCT complex with reovirus outer capsid protein sigma-3

SupramoleculeName: human TRiC/CCT complex with reovirus outer capsid protein sigma-3
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#9
Molecular weightTheoretical: 41 kDa/nm

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Supramolecule #2: human TRiC/CCT complex

SupramoleculeName: human TRiC/CCT complex / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#8
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #3: reovirus outer capsid protein sigma-3

SupramoleculeName: reovirus outer capsid protein sigma-3 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #9
Source (natural)Organism: Mammalian orthoreovirus 3 Dearing

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Macromolecule #1: T-complex protein 1 subunit epsilon

MacromoleculeName: T-complex protein 1 subunit epsilon / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 59.749957 KDa
Recombinant expressionOrganism: Insect cell expression vector pTIE1 (others)
SequenceString: MASMGTLAFD EYGRPFLIIK DQDRKSRLMG LEALKSHIMA AKAVANTMRT SLGPNGLDKM MVDKDGDVTV TNDGATILSM MDVDHQIAK LMVELSKSQD DEIGDGTTGV VVLAGALLEE AEQLLDRGIH PIRIADGYEQ AARVAIEHLD KISDSVLVDI K DTEPLIQT ...String:
MASMGTLAFD EYGRPFLIIK DQDRKSRLMG LEALKSHIMA AKAVANTMRT SLGPNGLDKM MVDKDGDVTV TNDGATILSM MDVDHQIAK LMVELSKSQD DEIGDGTTGV VVLAGALLEE AEQLLDRGIH PIRIADGYEQ AARVAIEHLD KISDSVLVDI K DTEPLIQT AKTTLGSKVV NSCHRQMAEI AVNAVLTVAD MERRDVDFEL IKVEGKVGGR LEDTKLIKGV IVDKDFSHPQ MP KKVEDAK IAILTCPFEP PKPKTKHKLD VTSVEDYKAL QKYEKEKFEE MIQQIKETGA NLAICQWGFD DEANHLLLQN NLP AVRWVG GPEIELIAIA TGGRIVPRFS ELTAEKLGFA GLVQEISFGT TKDKMLVIEQ CKNSRAVTIF IRGGNKMIIE EAKR SLHDA LCVIRNLIRD NRVVYGGGAA EISCALAVSQ EADKCPTLEQ YAMRAFADAL EVIPMALSEN SGMNPIQTMT EVRAR QVKE MNPALGIDCL HKGTNDMKQQ HVIETLIGKK QQISLATQMV RMILKIDDIR KPGESEE

UniProtKB: T-complex protein 1 subunit epsilon

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Macromolecule #2: T-complex protein 1 subunit beta

MacromoleculeName: T-complex protein 1 subunit beta / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 57.567141 KDa
Recombinant expressionOrganism: Insect cell expression vector pTIE1 (others)
SequenceString: MASLSLAPVN IFKAGADEER AETARLTSFI GAIAIGDLVK STLGPKGMDK ILLSSGRDAS LMVTNDGATI LKNIGVDNPA AKVLVDMSR VQDDEVGDGT TSVTVLAAEL LREAESLIAK KIHPQTIIAG WREATKAARE ALLSSAVDHG SDEVKFRQDL M NIAGTTLS ...String:
MASLSLAPVN IFKAGADEER AETARLTSFI GAIAIGDLVK STLGPKGMDK ILLSSGRDAS LMVTNDGATI LKNIGVDNPA AKVLVDMSR VQDDEVGDGT TSVTVLAAEL LREAESLIAK KIHPQTIIAG WREATKAARE ALLSSAVDHG SDEVKFRQDL M NIAGTTLS SKLLTHHKDH FTKLAVEAVL RLKGSGNLEA IHIIKKLGGS LADSYLDEGF LLDKKIGVNQ PKRIENAKIL IA NTGMDTD KIKIFGSRVR VDSTAKVAEI EHAEKEKMKE KVERILKHGI NCFINRQLIY NYPEQLFGAA GVMAIEHADF AGV ERLALV TGGEIASTFD HPELVKLGSC KLIEEVMIGE DKLIHFSGVA LGEACTIVLR GATQQILDEA ERSLHDALCV LAQT VKDSR TVYGGGCSEM LMAHAVTQLA NRTPGKEAVA MESYAKALRM LPTIIADNAG YDSADLVAQL RAAHSEGNTT AGLDM REGT IGDMAILGIT ESFQVKRQVL LSAAEAAEVI LRVDNIIKAA PRKRVPDHHP C

UniProtKB: T-complex protein 1 subunit beta

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Macromolecule #3: T-complex protein 1 subunit delta

MacromoleculeName: T-complex protein 1 subunit delta / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 57.996113 KDa
Recombinant expressionOrganism: Insect cell expression vector pTIE1 (others)
SequenceString: MPENVAPRSG ATAGAAGGRG KGAYQDRDKP AQIRFSNISA AKAVADAIRT SLGPKGMDKM IQDGKGDVTI TNDGATILKQ MQVLHPAAR MLVELSKAQD IEAGDGTTSV VIIAGSLLDS CTKLLQKGIH PTIISESFQK ALEKGIEILT DMSRPVELSD R ETLLNSAT ...String:
MPENVAPRSG ATAGAAGGRG KGAYQDRDKP AQIRFSNISA AKAVADAIRT SLGPKGMDKM IQDGKGDVTI TNDGATILKQ MQVLHPAAR MLVELSKAQD IEAGDGTTSV VIIAGSLLDS CTKLLQKGIH PTIISESFQK ALEKGIEILT DMSRPVELSD R ETLLNSAT TSLNSKVVSQ YSSLLSPMSV NAVMKVIDPA TATSVDLRDI KIVKKLGGTI DDCELVEGLV LTQKVSNSGI TR VEKAKIG LIQFCLSAPK TDMDNQIVVS DYAQMDRVLR EERAYILNLV KQIKKTGCNV LLIQKSILRD ALSDLALHFL NKM KIMVIK DIEREDIEFI CKTIGTKPVA HIDQFTADML GSAELAEEVN LNGSGKLLKI TGCASPGKTV TIVVRGSNKL VIEE AERSI HDALCVIRCL VKKRALIAGG GAPEIELALR LTEYSRTLSG MESYCVRAFA DAMEVIPSTL AENAGLNPIS TVTEL RNRH AQGEKTAGIN VRKGGISNIL EELVVQPLLV SVSALTLATE TVRSILKIDD VVNTR

UniProtKB: T-complex protein 1 subunit delta

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Macromolecule #4: T-complex protein 1 subunit gamma

MacromoleculeName: T-complex protein 1 subunit gamma / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 60.613855 KDa
Recombinant expressionOrganism: Insect cell expression vector pTIE1 (others)
SequenceString: MMGHRPVLVL SQNTKRESGR KVQSGNINAA KTIADIIRTC LGPKSMMKML LDPMGGIVMT NDGNAILREI QVQHPAAKSM IEISRTQDE EVGDGTTSVI ILAGEMLSVA EHFLEQQMHP TVVISAYRKA LDDMISTLKK ISIPVDISDS DMMLNIINSS I TTKAISRW ...String:
MMGHRPVLVL SQNTKRESGR KVQSGNINAA KTIADIIRTC LGPKSMMKML LDPMGGIVMT NDGNAILREI QVQHPAAKSM IEISRTQDE EVGDGTTSVI ILAGEMLSVA EHFLEQQMHP TVVISAYRKA LDDMISTLKK ISIPVDISDS DMMLNIINSS I TTKAISRW SSLACNIALD AVKMVQFEEN GRKEIDIKKY ARVEKIPGGI IEDSCVLRGV MINKDVTHPR MRRYIKNPRI VL LDSSLEY KKGESQTDIE ITREEDFTRI LQMEEEYIQQ LCEDIIQLKP DVVITEKGIS DLAQHYLMRA NITAIRRVRK TDN NRIARA CGARIVSRPE ELREDDVGTG AGLLEIKKIG DEYFTFITDC KDPKACTILL RGASKEILSE VERNLQDAMQ VCRN VLLDP QLVPGGGASE MAVAHALTEK SKAMTGVEQW PYRAVAQALE VIPRTLIQNC GASTIRLLTS LRAKHTQENC ETWGV NGET GTLVDMKELG IWEPLAVKLQ TYKTAVETAV LLLRIDDIVS GHKKKGDDQS RQGGAPDAGQ E

UniProtKB: T-complex protein 1 subunit gamma

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Macromolecule #5: T-complex protein 1 subunit eta

MacromoleculeName: T-complex protein 1 subunit eta / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 59.443535 KDa
Recombinant expressionOrganism: Insect cell expression vector pTIE1 (others)
SequenceString: MMPTPVILLK EGTDSSQGIP QLVSNISACQ VIAEAVRTTL GPRGMDKLIV DGRGKATISN DGATILKLLD VVHPAAKTLV DIAKSQDAE VGDGTTSVTL LAAEFLKQVK PYVEEGLHPQ IIIRAFRTAT QLAVNKIKEI AVTVKKADKV EQRKLLEKCA M TALSSKLI ...String:
MMPTPVILLK EGTDSSQGIP QLVSNISACQ VIAEAVRTTL GPRGMDKLIV DGRGKATISN DGATILKLLD VVHPAAKTLV DIAKSQDAE VGDGTTSVTL LAAEFLKQVK PYVEEGLHPQ IIIRAFRTAT QLAVNKIKEI AVTVKKADKV EQRKLLEKCA M TALSSKLI SQQKAFFAKM VVDAVMMLDD LLQLKMIGIK KVQGGALEDS QLVAGVAFKK TFSYAGFEMQ PKKYHNPKIA LL NVELELK AEKDNAEIRV HTVEDYQAIV DAEWNILYDK LEKIHHSGAK VVLSKLPIGD VATQYFADRD MFCAGRVPEE DLK RTMMAC GGSIQTSVNA LSADVLGRCQ VFEETQIGGE RYNFFTGCPK AKTCTFILRG GAEQFMEETE RSLHDAIMIV RRAI KNDSV VAGGGAIEME LSKYLRDYSR TIPGKQQLLI GAYAKALEII PRQLCDNAGF DATNILNKLR ARHAQGGTWY GVDIN NEDI ADNFEAFVWE PAMVRINALT AASEAACLIV SVDETIKNPR STVDAPTAAG RGRGRGRPH

UniProtKB: T-complex protein 1 subunit eta

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Macromolecule #6: T-complex protein 1 subunit theta

MacromoleculeName: T-complex protein 1 subunit theta / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 59.691422 KDa
Recombinant expressionOrganism: Insect cell expression vector pTIE1 (others)
SequenceString: MALHVPKAPG FAQMLKEGAK HFSGLEEAVY RNIQACKELA QTTRTAYGPN GMNKMVINHL EKLFVTNDAA TILRELEVQH PAAKMIVMA SHMQEQEVGD GTNFVLVFAG ALLELAEELL RIGLSVSEVI EGYEIACRKA HEILPNLVCC SAKNLRDIDE V SSLLRTSI ...String:
MALHVPKAPG FAQMLKEGAK HFSGLEEAVY RNIQACKELA QTTRTAYGPN GMNKMVINHL EKLFVTNDAA TILRELEVQH PAAKMIVMA SHMQEQEVGD GTNFVLVFAG ALLELAEELL RIGLSVSEVI EGYEIACRKA HEILPNLVCC SAKNLRDIDE V SSLLRTSI MSKQYGNEVF LAKLIAQACV SIFPDSGHFN VDNIRVCKIL GSGISSSSVL HGMVFKKETE GDVTSVKDAK IA VYSCPFD GMITETKGTV LIKTAEELMN FSKGEENLMD AQVKAIADTG ANVVVTGGKV ADMALHYANK YNIMLVRLNS KWD LRRLCK TVGATALPRL TPPVLEEMGH CDSVYLSEVG DTQVVVFKHE KEDGAISTIV LRGSTDNLMD DIERAVDDGV NTFK VLTRD KRLVPGGGAT EIELAKQITS YGETCPGLEQ YAIKKFAEAF EAIPRALAEN SGVKANEVIS KLYAVHQEGN KNVGL DIEA EVPAVKDMLE AGILDTYLGK YWAIKLATNA AVTVLRVDQI IMAKPAGGPK PPSGKKDWDD DQND

UniProtKB: T-complex protein 1 subunit theta

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Macromolecule #7: T-complex protein 1 subunit zeta

MacromoleculeName: T-complex protein 1 subunit zeta / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 58.106086 KDa
Recombinant expressionOrganism: Insect cell expression vector pTIE1 (others)
SequenceString: MAAVKTLNPK AEVARAQAAL AVNISAARGL QDVLRTNLGP KGTMKMLVSG AGDIKLTKDG NVLLHEMQIQ HPTASLIAKV ATAQDDITG DGTTSNVLII GELLKQADLY ISEGLHPRII TEGFEAAKEK ALQFLEEVKV SREMDRETLI DVARTSLRTK V HAELADVL ...String:
MAAVKTLNPK AEVARAQAAL AVNISAARGL QDVLRTNLGP KGTMKMLVSG AGDIKLTKDG NVLLHEMQIQ HPTASLIAKV ATAQDDITG DGTTSNVLII GELLKQADLY ISEGLHPRII TEGFEAAKEK ALQFLEEVKV SREMDRETLI DVARTSLRTK V HAELADVL TEAVVDSILA IKKQDEPIDL FMIEIMEMKH KSETDTSLIR GLVLDHGARH PDMKKRVEDA YILTCNVSLE YE KTEVNSG FFYKSAEERE KLVKAERKFI EDRVKKIIEL KRKVCGDSDK GFVVINQKGI DPFSLDALSK EGIVALRRAK RRN MERLTL ACGGVALNSF DDLSPDCLGH AGLVYEYTLG EEKFTFIEKC NNPRSVTLLI KGPNKHTLTQ IKDAVRDGLR AVKN AIDDG CVVPGAGAVE VAMAEALIKH KPSVKGRAQL GVQAFADALL IIPKVLAQNS GFDLQETLVK IQAEHSESGQ LVGVD LNTG EPMVAAEVGV WDNYCVKKQL LHSCTVIATN ILLVDEIMRA GMSSLKG

UniProtKB: T-complex protein 1 subunit zeta

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Macromolecule #8: T-complex protein 1 subunit alpha

MacromoleculeName: T-complex protein 1 subunit alpha / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 60.418477 KDa
Recombinant expressionOrganism: Insect cell expression vector pTIE1 (others)
SequenceString: MEGPLSVFGD RSTGETIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT ILKLLEVEHP AAKVLCELAD LQDKEVGDG TTSVVIIAAE LLKNADELVK QKIHPTSVIS GYRLACKEAV RYINENLIVN TDELGRDCLI NAAKTSMSSK I IGINGDFF ...String:
MEGPLSVFGD RSTGETIRSQ NVMAAASIAN IVKSSLGPVG LDKMLVDDIG DVTITNDGAT ILKLLEVEHP AAKVLCELAD LQDKEVGDG TTSVVIIAAE LLKNADELVK QKIHPTSVIS GYRLACKEAV RYINENLIVN TDELGRDCLI NAAKTSMSSK I IGINGDFF ANMVVDAVLA IKYTDIRGQP RYPVNSVNIL KAHGRSQMES MLISGYALNC VVGSQGMPKR IVNAKIACLD FS LQKTKMK LGVQVVITDP EKLDQIRQRE SDITKERIQK ILATGANVIL TTGGIDDMCL KYFVEAGAMA VRRVLKRDLK RIA KASGAT ILSTLANLEG EETFEAAMLG QAEEVVQERI CDDELILIKN TKARTSASII LRGANDFMCD EMERSLHDAL CVVK RVLES KSVVPGGGAV EAALSIYLEN YATSMGSREQ LAIAEFARSL LVIPNTLAVN AAQDSTDLVA KLRAFHNEAQ VNPER KNLK WIGLDLSNGK PRDNKQAGVF EPTIVKVKSL KFATEAAITI LRIDDLIKLH PESKDDKHGS YEDAVHSGAL ND

UniProtKB: T-complex protein 1 subunit alpha

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Macromolecule #9: Outer capsid protein sigma-3

MacromoleculeName: Outer capsid protein sigma-3 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Reovirus type 3 (strain Dearing) / Strain: Dearing
Molecular weightTheoretical: 41.168121 KDa
Recombinant expressionOrganism: Insect cell expression vector pTIE1 (others)
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 #10: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 10 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #11: water

MacromoleculeName: water / type: ligand / ID: 11 / Number of copies: 420 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER / Water

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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: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TALOS ARCTICA
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 36.0 e/Å2
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 6.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 26000

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