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- EMDB-0758: TRiC at 0.2 mM ADP-AlFx, Conformation 1, 0.2-C1 -

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ID or keywords:

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Basic information

Entry
Database: EMDB / ID: EMD-0758
TitleTRiC at 0.2 mM ADP-AlFx, Conformation 1, 0.2-C1
Map dataTRiC at 0.2 mM ADP-AlFx, Conformation 1, 0.2-C1
Sample
  • Complex: TRiC complex
    • Protein or peptide: x 8 types
  • Ligand: x 4 types
KeywordsChaperonin TRiC/CCT / Allosteric network / ATPase cycle / Conformational landscape / Cryo-EM / CHAPERONE
Function / homology
Function and homology information


Association of TriC/CCT with target proteins during biosynthesis / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / : / chaperone mediated protein folding independent of cofactor / chaperonin-containing T-complex / : / Neutrophil degranulation / ATP-dependent protein folding chaperone / unfolded protein binding / protein folding ...Association of TriC/CCT with target proteins during biosynthesis / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / : / chaperone mediated protein folding independent of cofactor / chaperonin-containing T-complex / : / Neutrophil degranulation / ATP-dependent protein folding chaperone / unfolded protein binding / protein folding / ATP hydrolysis activity / ATP binding / plasma membrane / cytoplasm
Similarity search - Function
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. ...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
T-complex protein 1 subunit alpha / T-complex protein 1 subunit beta / T-complex protein 1 subunit gamma / T-complex protein 1 subunit delta / T-complex protein 1 subunit zeta / T-complex protein 1 subunit epsilon / T-complex protein 1 subunit eta / T-complex protein 1 subunit theta
Similarity search - Component
Biological speciesSaccharomyces cerevisiae S288C (yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.99 Å
AuthorsJin M / Cong Y
Funding support China, 4 items
OrganizationGrant numberCountry
National Basic Research Program of China (973 Program)2017YFA0503503 China
National Natural Science Foundation of China31670754 China
National Natural Science Foundation of China31872714 China
National Natural Science Foundation of China31861143028 China
CitationJournal: Proc Natl Acad Sci U S A / Year: 2019
Title: An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.
Authors: Mingliang Jin / Wenyu Han / Caixuan Liu / Yunxiang Zang / Jiawei Li / Fangfang Wang / Yanxing Wang / Yao Cong /
Abstract: TRiC/CCT assists the folding of ∼10% of cytosolic proteins through an ATP-driven conformational cycle and is essential in maintaining protein homeostasis. Here, we determined an ensemble of cryo- ...TRiC/CCT assists the folding of ∼10% of cytosolic proteins through an ATP-driven conformational cycle and is essential in maintaining protein homeostasis. Here, we determined an ensemble of cryo-electron microscopy (cryo-EM) structures of yeast TRiC at various nucleotide concentrations, with 4 open-state maps resolved at near-atomic resolutions, and a closed-state map at atomic resolution, revealing an extra layer of an unforeseen N-terminal allosteric network. We found that, during TRiC ring closure, the CCT7 subunit moves first, responding to nucleotide binding; CCT4 is the last to bind ATP, serving as an ATP sensor; and CCT8 remains ADP-bound and is hardly involved in the ATPase-cycle in our experimental conditions; overall, yeast TRiC consumes nucleotide in a 2-ring positively coordinated manner. Our results depict a thorough picture of the TRiC conformational landscape and its allosteric transitions from the open to closed states in more structural detail and offer insights into TRiC subunit specificity in ATP consumption and ring closure, and potentially in substrate processing.
History
DepositionAug 23, 2019-
Header (metadata) releaseSep 18, 2019-
Map releaseSep 18, 2019-
UpdateMar 27, 2024-
Current statusMar 27, 2024Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.005
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.005
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6ks6
  • Surface level: 0.005
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_0758.png

Downloads & links

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Map

FileDownload / File: emd_0758.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationTRiC at 0.2 mM ADP-AlFx, Conformation 1, 0.2-C1
Voxel sizeX=Y=Z: 0.659 Å
Density
Contour LevelBy AUTHOR: 0.005 / Movie #1: 0.005
Minimum - Maximum-0.02401147 - 0.04818636
Average (Standard dev.)0.00008942386 (±0.0014266719)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 337.408 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.6590.6590.659
M x/y/z512512512
origin x/y/z0.0000.0000.000
length x/y/z337.408337.408337.408
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS512512512
D min/max/mean-0.0240.0480.000

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Supplemental data

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Sample components

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Entire : TRiC complex

EntireName: TRiC complex
Components
  • Complex: TRiC complex
    • Protein or peptide: T-complex protein 1 subunit alpha
    • 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 epsilon
    • Protein or peptide: fusion protein of T-complex protein 1 subunit gamma,rep-His-CBP and 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
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: ALUMINUM FLUORIDEAluminium fluoride
  • Ligand: water

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Supramolecule #1: TRiC complex

SupramoleculeName: TRiC complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8 / Details: TRiC complex at 0.2 mM ADP-AlFx
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
Molecular weightTheoretical: 960 KDa

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Macromolecule #1: T-complex protein 1 subunit alpha

MacromoleculeName: T-complex protein 1 subunit alpha / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: S288c
Molecular weightTheoretical: 60.557566 KDa
SequenceString: MSQLFNNSRS DTLFLGGEKI SGDDIRNQNV LATMAVANVV KSSLGPVGLD KMLVDDIGDF TVTNDGATIL SLLDVQHPAG KILVELAQQ QDREIGDGTT SVVIIASELL KRANELVKNK IHPTTIITGF RVALREAIRF INEVLSTSVD TLGKETLINI A KTSMSSKI ...String:
MSQLFNNSRS DTLFLGGEKI SGDDIRNQNV LATMAVANVV KSSLGPVGLD KMLVDDIGDF TVTNDGATIL SLLDVQHPAG KILVELAQQ QDREIGDGTT SVVIIASELL KRANELVKNK IHPTTIITGF RVALREAIRF INEVLSTSVD TLGKETLINI A KTSMSSKI IGADSDFFSN MVVDALLAVK TQNSKGEIKY PVKAVNVLKA HGKSATESLL VPGYALNCTV ASQAMPKRIA GG NVKIACL DLNLQKARMA MGVQINIDDP EQLEQIRKRE AGIVLERVKK IIDAGAQVVL TTKGIDDLCL KEFVEAKIMG VRR CKKEDL RRIARATGAT LVSSMSNLEG EETFESSYLG LCDEVVQAKF SDDECILIKG TSKHSSSSII LRGANDYSLD EMER SLHDS LSVVKRTLES GNVVPGGGCV EAALNIYLDN FATTVGSREQ LAIAEFAAAL LIIPKTLAVN AAKDSSELVA KLRSY HAAS QMAKPEDVKR RSYRNYGLDL IRGKIVDEIH AGVLEPTISK VKSLKSALEA CVAILRIDTM ITVDPEPPKE DPHDH

UniProtKB: T-complex protein 1 subunit alpha

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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: Saccharomyces cerevisiae S288C (yeast) / Strain: S288c
Molecular weightTheoretical: 57.276254 KDa
SequenceString: MSVQIFGDQV TEERAENARL SAFVGAIAVG DLVKSTLGPK GMDKLLQSAS SNTCMVTNDG ATILKSIPLD NPAAKVLVNI SKVQDDEVG DGTTSVTVLS AELLREAEKL IDQSKIHPQT IIEGYRLASA AALDALTKAA VDNSHDKTMF REDLIHIAKT T LSSKILSQ ...String:
MSVQIFGDQV TEERAENARL SAFVGAIAVG DLVKSTLGPK GMDKLLQSAS SNTCMVTNDG ATILKSIPLD NPAAKVLVNI SKVQDDEVG DGTTSVTVLS AELLREAEKL IDQSKIHPQT IIEGYRLASA AALDALTKAA VDNSHDKTMF REDLIHIAKT T LSSKILSQ DKDHFAELAT NAILRLKGST NLEHIQIIKI LGGKLSDSFL DEGFILAKKF GNNQPKRIEN AKILIANTTL DT DKVKIFG TKFKVDSTAK LAQLEKAERE KMKNKIAKIS KFGINTFINR QLIYDYPEQL FTDLGINSIE HADFEGVERL ALV TGGEVV STFDEPSKCK LGECDVIEEI MLGEQPFLKF SGCKAGEACT IVLRGATDQT LDEAERSLHD ALSVLSQTTK ETRT VLGGG CAEMVMSKAV DTEAQNIDGK KSLAVEAFAR ALRQLPTILA DNAGFDSSEL VSKLRSSIYN GISTSGLDLN NGTIA DMRQ LGIVESYKLK RAVVSSASEA AEVLLRVDNI IRARPRTANR QHM

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: Saccharomyces cerevisiae S288C (yeast) / Strain: S288c
Molecular weightTheoretical: 57.68241 KDa
SequenceString: MSAKVPSNAT FKNKEKPQEV RKANIIAARS VADAIRTSLG PKGMDKMIKT SRGEIIISND GHTILKQMAI LHPVARMLVE VSAAQDSEA GDGTTSVVIL TGALLGAAER LLNKGIHPTI IADSFQSAAK RSVDILLEMC HKVSLSDREQ LVRAASTSLS S KIVSQYSS ...String:
MSAKVPSNAT FKNKEKPQEV RKANIIAARS VADAIRTSLG PKGMDKMIKT SRGEIIISND GHTILKQMAI LHPVARMLVE VSAAQDSEA GDGTTSVVIL TGALLGAAER LLNKGIHPTI IADSFQSAAK RSVDILLEMC HKVSLSDREQ LVRAASTSLS S KIVSQYSS FLAPLAVDSV LKISDENSKN VDLNDIRLVK KVGGTIDDTE MIDGVVLTQT AIKSAGGPTR KEKAKIGLIQ FQ ISPPKPD TENNIIVNDY RQMDKILKEE RAYLLNICKK IKKAKCNVLL IQKSILRDAV NDLALHFLSK LNIMVVKDIE REE IEFLSK GLGCKPIADI ELFTEDRLGS ADLVEEIDSD GSKIVRVTGI RNNNARPTVS VVIRGANNMI IDETERSLHD ALCV IRCLV KERGLIAGGG APEIEISRRL SKEARSMEGV QAFIWQEFAS ALEVIPTTLA ENAGLNSIKV VTELRSKHEN GELND GISV RRSGTTNTYE EHILQPVLVS TSAITLASEC VKSILRIDDI AFSR

UniProtKB: T-complex protein 1 subunit delta

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Macromolecule #4: T-complex protein 1 subunit epsilon

MacromoleculeName: T-complex protein 1 subunit epsilon / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: S288c
Molecular weightTheoretical: 61.995004 KDa
SequenceString: MAARPQQPPM EMPDLSNAIV AQDEMGRPFI IVKDQGNKKR QHGLEAKKSH ILAARSVASI IKTSLGPRGL DKILISPDGE ITITNDGAT ILSQMELDNE IAKLLVQLSK SQDDEIGDGT TGVVVLASAL LDQALELIQK GIHPIKIANG FDEAAKLAIS K LEETCDDI ...String:
MAARPQQPPM EMPDLSNAIV AQDEMGRPFI IVKDQGNKKR QHGLEAKKSH ILAARSVASI IKTSLGPRGL DKILISPDGE ITITNDGAT ILSQMELDNE IAKLLVQLSK SQDDEIGDGT TGVVVLASAL LDQALELIQK GIHPIKIANG FDEAAKLAIS K LEETCDDI SASNDELFRD FLLRAAKTSL GSKIVSKDHD RFAEMAVEAV INVMDKDRKD VDFDLIKMQG RVGGSISDSK LI NGVILDK DFSHPQMPKC VLPKEGSDGV KLAILTCPFE PPKPKTKHKL DISSVEEYQK LQTYEQDKFK EMIDDVKKAG ADV VICQWG FDDEANHLLL QNDLPAVRWV GGQELEHIAI STNGRIVPRF QDLSKDKLGT CSRIYEQEFG TTKDRMLIIE QSKE TKTVT CFVRGSNKMI VDEAERALHD SLCVVRNLVK DSRVVYGGGA AEVTMSLAVS EEADKQRGID QYAFRGFAQA LDTIP MTLA ENSGLDPIGT LSTLKSKQLK EKISNIGVDC LGYGSNDMKE LFVVDPFIGK KQQILLATQL CRMILKIDNV IISGKD EY

UniProtKB: T-complex protein 1 subunit epsilon

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Macromolecule #5: fusion protein of T-complex protein 1 subunit gamma,rep-His-CBP a...

MacromoleculeName: fusion protein of T-complex protein 1 subunit gamma,rep-His-CBP and T-complex protein 1 subunit gamma
type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: S288c
Molecular weightTheoretical: 65.423387 KDa
SequenceString: MQAPVVFMNA SQERTTGRQA QISNITAAKA VADVIRTCLG PKAMLKMLLD PMGGLVLTND GHAILREIDV AHPAAKSMLE LSRTQDEEV GDGTTTVIIL AGEILAQCAP YLIEKNIHPV IIIQALKKAL TDALEVIKQV SKPVDVENDA AMKKLIQASI G TKYVIHWS ...String:
MQAPVVFMNA SQERTTGRQA QISNITAAKA VADVIRTCLG PKAMLKMLLD PMGGLVLTND GHAILREIDV AHPAAKSMLE LSRTQDEEV GDGTTTVIIL AGEILAQCAP YLIEKNIHPV IIIQALKKAL TDALEVIKQV SKPVDVENDA AMKKLIQASI G TKYVIHWS EKMCELALDA VKTVRKDLGQ TVEGEPNFEI DIKRYVRVEK IPGGDVLDSR VLKGVLLNKD VVHPKMSRHI EN PRVVLLD CPLEYKKGES QTNIEIEKEE DWNRILQIEE EQVQLMCEQI LAVRPTLVIT EKGVSDLAQH YLLKGGCSVL RRV KKSDNN RIARVTGATI VNRVEDLKES DVGTNCGLFK VEMIGDEYFS FLDNCKEPLE GSGSGWSHPQ FEKGSGKRRW KKNF IAVSA ANRFKKISSS GALGSGHHHH HHHHGSGLQK ACTIMLRGGS KDILNEIDRN LQDAMAVARN VMLSPSLSPG GGATE MAVS VKLAEKAKQL EGIQQWPYQA VADAMECIPR TLIQNAGGDP IRLLSQLRAK HAQGNFTTGI DGDKGKIVDM VSYGIW EPE VIKQQSVKTA IESACLLLRV DDIVSGVRKQ E

UniProtKB: T-complex protein 1 subunit gamma, T-complex protein 1 subunit gamma

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Macromolecule #6: T-complex protein 1 subunit eta

MacromoleculeName: T-complex protein 1 subunit eta / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: S288c
Molecular weightTheoretical: 59.802438 KDa
SequenceString: MNFGSQTPTI VVLKEGTDAS QGKGQIISNI NACVAVQEAL KPTLGPLGSD ILIVTSNQKT TISNDGATIL KLLDVVHPAA KTLVDISRA QDAEVGDGTT SVTILAGELM KEAKPFLEEG ISSHLIMKGY RKAVSLAVEK INELAVDITS EKSSGRELLE R CARTAMSS ...String:
MNFGSQTPTI VVLKEGTDAS QGKGQIISNI NACVAVQEAL KPTLGPLGSD ILIVTSNQKT TISNDGATIL KLLDVVHPAA KTLVDISRA QDAEVGDGTT SVTILAGELM KEAKPFLEEG ISSHLIMKGY RKAVSLAVEK INELAVDITS EKSSGRELLE R CARTAMSS KLIHNNADFF VKMCVDAVLS LDRNDLDDKL IGIKKIPGGA MEESLFINGV AFKKTFSYAG FEQQPKKFNN PK ILSLNVE LELKAEKDNA EVRVEHVEDY QAIVDAEWQL IFEKLRQVEE TGANIVLSKL PIGDLATQFF ADRNIFCAGR VSA DDMNRV IQAVGGSIQS TTSDIKPEHL GTCALFEEMQ IGSERYNLFQ GCPQAKTCTL LLRGGAEQVI AEVERSLHDA IMIV KRALQ NKLIVAGGGA TEMEVSKCLR DYSKTIAGKQ QMIINAFAKA LEVIPRQLCE NAGFDAIEIL NKLRLAHSKG EKWYG VVFE TENIGDNFAK FVWEPALVKI NALNSATEAT NLILSVDETI TNKGSESANA GMMPPQGAGR GRGMPM

UniProtKB: T-complex protein 1 subunit eta

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Macromolecule #7: T-complex protein 1 subunit theta

MacromoleculeName: T-complex protein 1 subunit theta / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: S288c
Molecular weightTheoretical: 61.735102 KDa
SequenceString: MSLRLPQNPN AGLFKQGYNS YSNADGQIIK SIAAIRELHQ MCLTSMGPCG RNKIIVNHLG KIIITNDAAT MLRELDIVHP AVKVLVMAT EQQKIDMGDG TNLVMILAGE LLNVSEKLIS MGLSAVEIIQ GYNMARKFTL KELDEMVVGE ITDKNDKNEL L KMIKPVIS ...String:
MSLRLPQNPN AGLFKQGYNS YSNADGQIIK SIAAIRELHQ MCLTSMGPCG RNKIIVNHLG KIIITNDAAT MLRELDIVHP AVKVLVMAT EQQKIDMGDG TNLVMILAGE LLNVSEKLIS MGLSAVEIIQ GYNMARKFTL KELDEMVVGE ITDKNDKNEL L KMIKPVIS SKKYGSEDIL SELVSEAVSH VLPVAQQAGE IPYFNVDSIR VVKIMGGSLS NSTVIKGMVF NREPEGHVKS LS EDKKHKV AVFTCPLDIA NTETKGTVLL HNAQEMLDFS KGEEKQIDAM MKEIADMGVE CIVAGAGVGE LALHYLNRYG ILV LKVPSK FELRRLCRVC GATPLPRLGA PTPEELGLVE TVKTMEIGGD RVTVFKQEQG EISRTSTIIL RGATQNNLDD IERA IDDGV AAVKGLMKPS GGKLLPGAGA TEIELISRIT KYGERTPGLL QLAIKQFAVA FEVVPRTLAE TAGLDVNEVL PNLYA AHNV TEPGAVKTDH LYKGVDIDGE SDEGVKDIRE ENIYDMLATK KFAINVATEA ATTVLSIDQI IMAKKAGGPR APQGPR PGN WDQED

UniProtKB: T-complex protein 1 subunit theta

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Macromolecule #8: T-complex protein 1 subunit zeta

MacromoleculeName: T-complex protein 1 subunit zeta / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: S288c
Molecular weightTheoretical: 59.997559 KDa
SequenceString: MSLQLLNPKA ESLRRDAALK VNVTSAEGLQ SVLETNLGPK GTLKMLVDGA GNIKLTKDGK VLLTEMQIQS PTAVLIARAA AAQDEITGD GTTTVVCLVG ELLRQAHRFI QEGVHPRIIT DGFEIARKES MKFLDEFKIS KTNLSNDREF LLQVARSSLL T KVDADLTE ...String:
MSLQLLNPKA ESLRRDAALK VNVTSAEGLQ SVLETNLGPK GTLKMLVDGA GNIKLTKDGK VLLTEMQIQS PTAVLIARAA AAQDEITGD GTTTVVCLVG ELLRQAHRFI QEGVHPRIIT DGFEIARKES MKFLDEFKIS KTNLSNDREF LLQVARSSLL T KVDADLTE VLTPIVTDAV LSVYDAQADN LDLHMVEIMQ MQHLSPKDTT FIKGLVLDHG GRHPDMPTRV KNAYVLILNV SL EYEKTEV NSGFFYSSAD QRDKLAASER KFVDAKLKKI IDLKNEVCGM DPDKGFVIIN QKGIDPMSLD VFAKHNILAL RRA KRRNME RLQLVTGGEA QNSVEDLSPQ ILGFSGLVYQ ETIGEEKFTY VTENTDPKSC TILIKGSTHY ALAQTKDAVR DGLR AVANV LKDKNIIPGA GAFYIALSRY LRSANMNKLG AKGKTKTGIE AFAEALLVIP KTLVKNSGFD PLDVLAMVED ELDDA QDSD ETRYVGVDLN IGDSCDPTIE GIWDSYRVLR NAITGATGIA SNLLLCDELL RAGRSTLKET PQ

UniProtKB: T-complex protein 1 subunit zeta

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Macromolecule #9: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 9 / Number of copies: 16 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

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Macromolecule #10: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 10 / Number of copies: 16 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #11: ALUMINUM FLUORIDE

MacromoleculeName: ALUMINUM FLUORIDE / type: ligand / ID: 11 / Number of copies: 14 / Formula: AF3
Molecular weightTheoretical: 83.977 Da
Chemical component information

ChemComp-AF3:
ALUMINUM FLUORIDE / Aluminium fluoride

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Macromolecule #12: water

MacromoleculeName: water / type: ligand / ID: 12 / Number of copies: 14 / 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

Concentration1 mg/mL
BufferpH: 7.5
VitrificationCryogen name: ETHANE

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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
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 38.0 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:

4v8r

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.99 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 277360

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