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- EMDB-23527: Cryo-EM structure of the yeast THO-Sub2 complex -

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Basic information

Entry
Database: EMDB / ID: EMD-23527
TitleCryo-EM structure of the yeast THO-Sub2 complex
Map data
Sample
  • Complex: THO-Sub2
    • Complex: Sub2
      • Protein or peptide: ATP-dependent RNA helicase SUB2
    • Complex: THO
      • Protein or peptide: THO complex subunit HPR1
      • Protein or peptide: THO complex subunit THP2
      • Protein or peptide: THO complex subunit 2
      • Protein or peptide: THO complex subunit MFT1
    • Complex: Tex1
      • Protein or peptide: Tex1
Keywordsnuclear mRNA export / DEAD-box ATPase / mRNP remodeling / RNA BINDING PROTEIN
Function / homology
Function and homology information


nucleoplasmic THO complex / THO complex part of transcription export complex / positive regulation of transcription elongation by RNA polymerase I / transcription export complex / Cdc73/Paf1 complex / : / mRNA 3'-end processing / positive regulation of transcription by RNA polymerase I / subtelomeric heterochromatin formation / transcription-coupled nucleotide-excision repair ...nucleoplasmic THO complex / THO complex part of transcription export complex / positive regulation of transcription elongation by RNA polymerase I / transcription export complex / Cdc73/Paf1 complex / : / mRNA 3'-end processing / positive regulation of transcription by RNA polymerase I / subtelomeric heterochromatin formation / transcription-coupled nucleotide-excision repair / mRNA export from nucleus / stress granule assembly / transcription elongation by RNA polymerase II / spliceosomal complex / mRNA splicing, via spliceosome / mRNA processing / DNA recombination / RNA helicase activity / chromosome, telomeric region / nucleic acid binding / molecular adaptor activity / RNA helicase / mRNA binding / ATP hydrolysis activity / RNA binding / ATP binding / nucleus / cytoplasm
Similarity search - Function
THO complex subunit Thp2 / Tho complex subunit THP2 / THO complex subunit 7/Mft1 / THO complex, subunitTHOC2, C-terminal / THO complex, subunitTHOC2, N-terminal / THO complex subunit 2, N-terminal domain / THO complex subunit 2 / Tho complex subunit 7 / Transcription factor/nuclear export subunit protein 2 / Transcription- and export-related complex subunit ...THO complex subunit Thp2 / Tho complex subunit THP2 / THO complex subunit 7/Mft1 / THO complex, subunitTHOC2, C-terminal / THO complex, subunitTHOC2, N-terminal / THO complex subunit 2, N-terminal domain / THO complex subunit 2 / Tho complex subunit 7 / Transcription factor/nuclear export subunit protein 2 / Transcription- and export-related complex subunit / THO complex subunit 2 N-terminus / THO complex, subunit THOC1 / THO complex subunit 1 transcription elongation factor / RNA helicase, DEAD-box type, Q motif / DEAD-box RNA helicase Q motif profile. / DEAD/DEAH box helicase / DEAD/DEAH box helicase domain / Helicase conserved C-terminal domain / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
THO complex subunit THP2 / THO complex subunit HPR1 / THO complex subunit MFT1 / THO complex subunit 2 / ATP-dependent RNA helicase SUB2
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast) / Saccharomyces bayanus (yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsXie Y / Ren Y
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM133743 United States
CitationJournal: Elife / Year: 2021
Title: Cryo-EM structure of the yeast TREX complex and coordination with the SR-like protein Gbp2.
Authors: Yihu Xie / Bradley P Clarke / Yong Joon Kim / Austin L Ivey / Pate S Hill / Yi Shi / Yi Ren /
Abstract: The evolutionarily conserved TRanscript-EXport (TREX) complex plays central roles during mRNP (messenger ribonucleoprotein) maturation and export from the nucleus to the cytoplasm. In yeast, TREX is ...The evolutionarily conserved TRanscript-EXport (TREX) complex plays central roles during mRNP (messenger ribonucleoprotein) maturation and export from the nucleus to the cytoplasm. In yeast, TREX is composed of the THO sub-complex (Tho2, Hpr1, Tex1, Mft1, and Thp2), the DEAD box ATPase Sub2, and Yra1. Here we present a 3.7 Å cryo-EM structure of the yeast THO•Sub2 complex. The structure reveals the intimate assembly of THO revolving around its largest subunit Tho2. THO stabilizes a semi-open conformation of the Sub2 ATPase via interactions with Tho2. We show that THO interacts with the serine-arginine (SR)-like protein Gbp2 through both the RS domain and RRM domains of Gbp2. Cross-linking mass spectrometry analysis supports the extensive interactions between THO and Gbp2, further revealing that RRM domains of Gbp2 are in close proximity to the C-terminal domain of Tho2. We propose that THO serves as a landing pad to configure Gbp2 to facilitate its loading onto mRNP.
History
DepositionFeb 23, 2021-
Header (metadata) releaseApr 14, 2021-
Map releaseApr 14, 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: 0.009
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.009
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7luv
  • Surface level: 0.009
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_23527.png

Downloads & links

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Map

FileDownload / File: emd_23527.map.gz / Format: CCP4 / Size: 476.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 0.6811 Å
Density
Contour LevelBy AUTHOR: 0.009 / Movie #1: 0.009
Minimum - Maximum-0.014631633 - 0.035607513
Average (Standard dev.)0.00015237037 (±0.0012308055)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions500500500
Spacing500500500
CellA=B=C: 340.55002 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.68110.68110.6811
M x/y/z500500500
origin x/y/z0.0000.0000.000
length x/y/z340.550340.550340.550
α/β/γ90.00090.00090.000
start NX/NY/NZ645365
NX/NY/NZ139143124
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS500500500
D min/max/mean-0.0150.0360.000

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Supplemental data

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Additional map: Assembly composed of four copies of the THO-Sub2 complex.

Fileemd_23527_additional_1.map
AnnotationAssembly composed of four copies of the THO-Sub2 complex.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : THO-Sub2

EntireName: THO-Sub2
Components
  • Complex: THO-Sub2
    • Complex: Sub2
      • Protein or peptide: ATP-dependent RNA helicase SUB2
    • Complex: THO
      • Protein or peptide: THO complex subunit HPR1
      • Protein or peptide: THO complex subunit THP2
      • Protein or peptide: THO complex subunit 2
      • Protein or peptide: THO complex subunit MFT1
    • Complex: Tex1
      • Protein or peptide: Tex1

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Supramolecule #1: THO-Sub2

SupramoleculeName: THO-Sub2 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all

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Supramolecule #2: Sub2

SupramoleculeName: Sub2 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #6
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #3: THO

SupramoleculeName: THO / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #1-#4
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #4: Tex1

SupramoleculeName: Tex1 / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #5
Source (natural)Organism: Saccharomyces bayanus (yeast)

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Macromolecule #1: THO complex subunit HPR1

MacromoleculeName: THO complex subunit HPR1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 71.126195 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MSNTEELIQN SIGFLQKTFK ALPVSFDSIR HEPLPSSMLH ASVLNFEWEP LEKNISAIHD RDSLIDIILK RFIIDSMTNA IEDEEENNL EKGLLNSCIG LDFVYNSRFN RSNPASWGNT FFELFSTIID LLNSPSTFLK FWPYAESRIE WFKMNTSVEP V SLGESNLI ...String:
MSNTEELIQN SIGFLQKTFK ALPVSFDSIR HEPLPSSMLH ASVLNFEWEP LEKNISAIHD RDSLIDIILK RFIIDSMTNA IEDEEENNL EKGLLNSCIG LDFVYNSRFN RSNPASWGNT FFELFSTIID LLNSPSTFLK FWPYAESRIE WFKMNTSVEP V SLGESNLI SYKQPLYEKL RHWNDILAKL ENNDILNTVK HYNMKYKLEN FLSELLPINE ESNFNRSASI SALQESDNEW NR SARERES NRSSDVIFAA DYNFVFYHLI ICPIEFAFSD LEYKNDVDRS LSPLLDAILE IEENFYSKIK MNNRTRYSLE EAL NTEYYA NYDVMTPKLP VYMKHSNAMK MDRNEFWANL QNIKESDDYT LRPTIMDISL SNTTCLYKQL TQEDDDYYRK QFIL QLCFT TNLIRNLISS DETRNFYKSC YLRENPLSDI DFENLDEVNK KRGLNLCSYI CDNRVLKFYK IKDPDFYRVI RKLMS SDEK FTTAKIDGFK EFQNFRISKE KIPPPAFDET FKKFTFIKMG NKLINNVWKI PTGLDKIEQE VKKPEGVYEA AQAKWE SKI SSETSGGEAK DEIIRQWQTL RFLRSRYLFD FDKVNEKTGV

UniProtKB: THO complex subunit HPR1

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Macromolecule #2: THO complex subunit THP2

MacromoleculeName: THO complex subunit THP2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 30.340264 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MTKEEGRTYF ESLCEEEQSL QESQTHLLNI LDILSVLADP RSSDDLLTES LKKLPDLHRE LINSSIRLRY DKYQTREAQL LEDTKTGRD VAAGVQNPKS ISEYYSTFEH LNRDTLRYIN LLKRLSVDLA KQVEVSDPSV TVYEMDKWVP SEKLQGILEQ Y CAPDTDIR ...String:
MTKEEGRTYF ESLCEEEQSL QESQTHLLNI LDILSVLADP RSSDDLLTES LKKLPDLHRE LINSSIRLRY DKYQTREAQL LEDTKTGRD VAAGVQNPKS ISEYYSTFEH LNRDTLRYIN LLKRLSVDLA KQVEVSDPSV TVYEMDKWVP SEKLQGILEQ Y CAPDTDIR GVDAQIKNYL DQIKMARAKF GLENKYSLKE RLSTLTKELN HWRKEWDDIE MLMFGDDAHS MKKMIQKIDS LK SEINAPS ESYPVDKEGD IVLE

UniProtKB: THO complex subunit THP2

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Macromolecule #3: THO complex subunit 2

MacromoleculeName: THO complex subunit 2 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 138.881453 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: GAMGSMAEQT LLSKLNALSQ KVIPPASPSQ ASILTEEVIR N(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)ESN DEKEDWLRTL FIELFDFINK (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) ...String:
GAMGSMAEQT LLSKLNALSQ KVIPPASPSQ ASILTEEVIR N(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)ESN DEKEDWLRTL FIELFDFINK (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)LTTISLCKL IPSLHE ELF KFSWISSKLL NKEQTTLLRH LLKKSKYELK KYNLLVENSV GYGQLVALLI LAYYDPDNFS KVSAYLKEIY HIMGKYS LD SIRTLDVILN VSSQFITEGY KFFIALLRKS DSWPSSHVAN NSNYSSLNEG GNMIAANIIS FNLSQYNEEV DKENYERY M DMCCILLKNG FVNFYSIWDN VKPEMEFLQE YIQNLETELE EESTKGVENP LAMAAALSTE NETDEDNALV VNDDVNMKD KISEETNADI ESKGKQKTQQ DILLFGKIKL LERLLIHGCV IPVIHVLKQY PKVLYVSESL SRYLGRVFEY LLNPLYTSMT SSGESKDMA TALMITRIDN GILAHKPRLI HKYKTHEPFE SLELNSSYVF YYSEWNSNLT PFASVNDLFE NSHIYLSIIG P YLGRIPTL LSKISRIGVA DIQKNHGSES LHVTIDKWID YVRKFIFPAT SLLQNNPIAT SEVYELMKFF PFEKRYFIYN EM MTKLSQD ILPLKVSFNK AEREAKSILK ALSIDTIAKE SRRFAKLIST NPLASLVPAV KQIENYDKVS ELVVYTTKYF NDF AYDVLQ FVLLLRLTYN RPAVQFDGVN QAMWVQRLSI FIAGLAKNCP NMDISNIITY ILKTLHNGNI IAVSILKELI ITVG GIRDL NEVNMKQLLM LNSGSPLKQY ARHLIYDFRD DNSVISSRLT SFFTDQSAIS EIILLLYTLN LKANTQNSHY KILST RCDE MNTLLWSFIE LIKHCLKGKA FEENVLPFVE LNNRFHLSTP WTFHIWRDYL DN(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)LKTLLFC CTSSEAGN L GLFFTDVLKK LEKMRLNGDF NDQASRKLYE WHSVITEQVI DLLSEKNYMS IRNGIEFMKH VTSVFPVVKA HIQLVYTTL EENLINEERE DIKLPSSALI GHLKARLKDA LELDEFCTLT EEEAEQKRIR EMELEEIKNY ETACQNEQKQ VALRKQLELN KSQRLQND

UniProtKB: THO complex subunit 2

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Macromolecule #4: THO complex subunit MFT1

MacromoleculeName: THO complex subunit MFT1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 29.46748 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MPLSQKQIDQ VRTKVHYSEV DTPFNKYLDI LGKVTKLTGS IINGTLSNDD SKIEKLTEQN ISQLKESAHL RFLDLQSSID TKKVADENW ETCQQETLAK LENLKDKLPD IKSIHSKLLL RIGKLQGLYD SVQVINREVE GLSEGRTSLV VTRAEWEKEL G TDLVKFLI ...String:
MPLSQKQIDQ VRTKVHYSEV DTPFNKYLDI LGKVTKLTGS IINGTLSNDD SKIEKLTEQN ISQLKESAHL RFLDLQSSID TKKVADENW ETCQQETLAK LENLKDKLPD IKSIHSKLLL RIGKLQGLYD SVQVINREVE GLSEGRTSLV VTRAEWEKEL G TDLVKFLI EKNYLKLVDP GLKKDSSEER YRIYDDFSKG PKELESINAS MKSDIENVRQ EVSSYKEKWL RDAEIFGKIT SI FKEELLK RDGLLNEAE

UniProtKB: THO complex subunit MFT1

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Macromolecule #5: Tex1

MacromoleculeName: Tex1 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces bayanus (yeast)
Molecular weightTheoretical: 41.248668 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) ...String:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)SLKF HASGSSMAYS RMDGSLTVWF IKDASFDKSV KVYIPD CCG SDKLATDLSW NPTSLNQMAV VSNSSEISLL LINEITLTAS KLRTLSLGSK TKVNSCLYDP LGNWLLAATK SEKIYLF NV KEDHRLVHSL NVNDISPNTN DVVYSIAWNN NGSHIFVGFK SGHLVILKLR DEMLEVSTKI KAHTSSITGI KIDPWGRY F VTGSSDGNCY IWSLKSLCCE KIIQDLDSAV VALDVCHLGK ILGVCTEDEM VYFYDLNEAK LLESKSLANH KSDLVLKFY PDKSWYILSG KNDTLSNHFV KNEKNLITYW KDM

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Macromolecule #6: ATP-dependent RNA helicase SUB2

MacromoleculeName: ATP-dependent RNA helicase SUB2 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO / EC number: RNA helicase
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 50.375859 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MSHEGEEDLL EYSDNEQEIQ IDASKAAEAG ETGAATSATE GDNNNNTAAG DKKGSYVGIH STGFKDFLLK PELSRAIIDC GFEHPSEVQ QHTIPQSIHG TDVLCQAKSG LGKTAVFVLS TLQQLDPVPG EVAVVVICNA RELAYQIRNE YLRFSKYMPD V KTAVFYGG ...String:
MSHEGEEDLL EYSDNEQEIQ IDASKAAEAG ETGAATSATE GDNNNNTAAG DKKGSYVGIH STGFKDFLLK PELSRAIIDC GFEHPSEVQ QHTIPQSIHG TDVLCQAKSG LGKTAVFVLS TLQQLDPVPG EVAVVVICNA RELAYQIRNE YLRFSKYMPD V KTAVFYGG TPISKDAELL KNKDTAPHIV VATPGRLKAL VREKYIDLSH VKNFVIDECD KVLEELDMRR DVQEIFRATP RD KQVMMFS ATLSQEIRPI CRRFLQNPLE IFVDDEAKLT LHGLQQYYIK LEEREKNRKL AQLLDDLEFN QVIIFVKSTT RAN ELTKLL NASNFPAITV HGHMKQEERI ARYKAFKDFE KRICVSTDVF GRGIDIERIN LAINYDLTNE ADQYLHRVGR AGRF GTKGL AISFVSSKED EEVLAKIQER FDVKIAEFPE EGIDPSTYLN N

UniProtKB: ATP-dependent RNA helicase SUB2

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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
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: FEI FALCON III (4k x 4k) / Average electron dose: 50.0 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:

5sup

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 30066

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: AB INITIO MODEL / Overall B value: 114.5
Output model

PDB-7luv:
Cryo-EM structure of the yeast THO-Sub2 complex

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