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- EMDB-33920: yeast TRiC-plp2-actin complex at S4 closed TRiC state -

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Basic information

Entry
Database: EMDB / ID: EMD-33920
Titleyeast TRiC-plp2-actin complex at S4 closed TRiC state
Map data
Sample
  • Complex: yeast TRiC-plp2-actin complex at C4 closed TRiC state
    • Complex: TRiC
      • Protein or peptide: x 8 types
    • Complex: plp2
      • Protein or peptide: x 1 types
  • Ligand: x 4 types
KeywordsTRiC/CCT / actin / phosducin-like protein / CHAPERONE
Function / homology
Function and homology information


cellular response to pheromone / negative regulation of chaperone-mediated 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 / negative regulation of signal transduction / Neutrophil degranulation / ATP-dependent protein folding chaperone / G-protein beta/gamma-subunit complex binding ...cellular response to pheromone / negative regulation of chaperone-mediated 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 / negative regulation of signal transduction / Neutrophil degranulation / ATP-dependent protein folding chaperone / G-protein beta/gamma-subunit complex binding / unfolded protein binding / protein folding / actin binding / actin cytoskeleton organization / regulation of cell cycle / positive regulation of transcription by RNA polymerase II / 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. ...: / 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 / Thioredoxin-like superfamily
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 / Phosducin-like protein 2
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsHan WY
Funding support China, 1 items
OrganizationGrant numberCountry
Chinese Academy of Sciences China
CitationJournal: Sci Adv / Year: 2023
Title: Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT.
Authors: Wenyu Han / Mingliang Jin / Caixuan Liu / Qiaoyu Zhao / Shutian Wang / Yifan Wang / Yue Yin / Chao Peng / Yanxing Wang / Yao Cong /
Abstract: The cytoskeletal proteins tubulin and actin are the obligate substrates of TCP-1 ring complex/Chaperonin containing TCP-1 (TRiC/CCT), and their folding involves co-chaperone. Through cryo-electron ...The cytoskeletal proteins tubulin and actin are the obligate substrates of TCP-1 ring complex/Chaperonin containing TCP-1 (TRiC/CCT), and their folding involves co-chaperone. Through cryo-electron microscopy analysis, we present a more complete picture of TRiC-assisted tubulin/actin folding along TRiC adenosine triphosphatase cycle, under the coordination of co-chaperone plp2. In the open S1/S2 states, plp2 and tubulin/actin engaged within opposite TRiC chambers. Notably, we captured an unprecedented TRiC-plp2-tubulin complex in the closed S3 state, engaged with a folded full-length -tubulin and loaded with a guanosine triphosphate, and a plp2 occupying opposite rings. Another closed S4 state revealed an actin in the intermediate folding state and a plp2. Accompanying TRiC ring closure, plp2 translocation could coordinate substrate translocation on the CCT6 hemisphere, facilitating substrate stabilization and folding. Our findings reveal the folding mechanism of the major cytoskeletal proteins tubulin/actin under the coordination of the biogenesis machinery TRiC and plp2 and extend our understanding of the links between cytoskeletal proteostasis and related human diseases.
History
DepositionJul 27, 2022-
Header (metadata) releaseMar 29, 2023-
Map releaseMar 29, 2023-
UpdateJul 3, 2024-
Current statusJul 3, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_33920.png

Downloads & links

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Map

FileDownload / File: emd_33920.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.32 Å/pix.
x 256 pix.
= 337.408 Å		1.32 Å/pix.
x 256 pix.
= 337.408 Å		1.32 Å/pix.
x 256 pix.
= 337.408 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.318 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.2
Minimum - Maximum-0.050628837 - 1.9850994
Average (Standard dev.)0.0069436873 (±0.06536454)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 337.408 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_33920_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_33920_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : yeast TRiC-plp2-actin complex at C4 closed TRiC state

EntireName: yeast TRiC-plp2-actin complex at C4 closed TRiC state
Components
  • Complex: yeast TRiC-plp2-actin complex at C4 closed TRiC state
    • Complex: TRiC
      • 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: 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
    • Complex: plp2
      • Protein or peptide: Phosducin-like protein 2
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: ALUMINUM FLUORIDE
  • Ligand: water

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Supramolecule #1: yeast TRiC-plp2-actin complex at C4 closed TRiC state

SupramoleculeName: yeast TRiC-plp2-actin complex at C4 closed TRiC state / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#9
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #2: TRiC

SupramoleculeName: TRiC / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#8
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #3: plp2

SupramoleculeName: plp2 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #9

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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 (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 60.557566 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
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 (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 57.276254 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
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 (brewer's yeast)
Molecular weightTheoretical: 57.68241 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
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 (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 61.995004 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
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: T-complex protein 1 subunit gamma

MacromoleculeName: T-complex protein 1 subunit gamma / type: protein_or_peptide / ID: 5
Details: fusion protein of T-complex protein 1 subunit gamma,rep-His-CBP and T-complex protein 1 subunit gamma
Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 65.423387 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
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 (brewer's yeast)
Molecular weightTheoretical: 59.802438 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
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 (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 61.735102 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
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 (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 59.997559 KDa
Recombinant expressionOrganism: Saccharomyces cerevisiae (brewer's yeast)
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: Phosducin-like protein 2

MacromoleculeName: Phosducin-like protein 2 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 32.83627 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MQNEPMFQVQ VDESEDSEWN DILRAKGVIP ERAPSPTAKL EEALEEAIAK QHENRLEDKD LSDLEELEDD EDEDFLEAYK IKRLNEIRK LQERSKFGEV FHINKPEYNK EVTLASQGKK YEGAQTNDNG EEDDGGVYVF VHLSLQSKLQ SRILSHLFQS A ACKFREIK ...String:
MQNEPMFQVQ VDESEDSEWN DILRAKGVIP ERAPSPTAKL EEALEEAIAK QHENRLEDKD LSDLEELEDD EDEDFLEAYK IKRLNEIRK LQERSKFGEV FHINKPEYNK EVTLASQGKK YEGAQTNDNG EEDDGGVYVF VHLSLQSKLQ SRILSHLFQS A ACKFREIK FVEIPANRAI ENYPESNCPT LIVYYRGEVI KNMITLLELG GNNSKMEDFE DFMVKVGAVA EGDNRLIMNR DD EESREER KLHYGEKKSI RSGIRGKFNV GIGGNDDGNI NDDDDGFFD

UniProtKB: Phosducin-like protein 2

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Macromolecule #10: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 10 / Number of copies: 16 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

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

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Macromolecule #11: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 11 / Number of copies: 16 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #12: ALUMINUM FLUORIDE

MacromoleculeName: ALUMINUM FLUORIDE / type: ligand / ID: 12 / Number of copies: 14 / Formula: AF3
Molecular weightTheoretical: 83.977 Da
Chemical component information

ChemComp-AF3:
ALUMINUM FLUORIDE

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Macromolecule #13: water

MacromoleculeName: water / type: ligand / ID: 13 / Number of copies: 14 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
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 TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 38.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: EMDB MAP
EMDB ID:

0758

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 58195
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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