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- EMDB-14804: Structure of an endogenous human TREX complex bound to mRNA, comp... -

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Basic information

Entry
Database: EMDB / ID: EMD-14804
TitleStructure of an endogenous human TREX complex bound to mRNA, composite map
Map dataTREX-mRNA composite map generated from sharpened focused maps A (EMD 14805),B (EMD-14806) and C (EMD-14807 )
Sample
  • Complex: endogenous human TREX-mRNA complex
    • RNA: RNA
    • Protein or peptide: THO complex subunit 1
    • Protein or peptide: THO complex subunit 2
    • Protein or peptide: THO complex subunit 3
    • Protein or peptide: THO complex subunit 5 homolog
    • Protein or peptide: THO complex subunit 6 homolog
    • Protein or peptide: THO complex subunit 7 homolog
    • Protein or peptide: Spliceosome RNA helicase DDX39B
    • Protein or peptide: THO complex subunit 4
Function / homology
Function and homology information


THO complex / THO complex part of transcription export complex / primitive hemopoiesis / transcription export complex / C5-methylcytidine-containing RNA reader activity / regulation of mRNA export from nucleus / U6 snRNP / RNA secondary structure unwinding / stem cell division / Transport of the SLBP independent Mature mRNA ...THO complex / THO complex part of transcription export complex / primitive hemopoiesis / transcription export complex / C5-methylcytidine-containing RNA reader activity / regulation of mRNA export from nucleus / U6 snRNP / RNA secondary structure unwinding / stem cell division / Transport of the SLBP independent Mature mRNA / Transport of the SLBP Dependant Mature mRNA / mRNA 3'-end processing / ATP-dependent activity, acting on RNA / ATP-dependent protein binding / Transport of Mature mRNA Derived from an Intronless Transcript / U4 snRNA binding / RNA export from nucleus / Transport of Mature mRNA derived from an Intron-Containing Transcript / positive regulation of DNA-templated transcription, elongation / U4 snRNP / RNA Polymerase II Transcription Termination / poly(A)+ mRNA export from nucleus / generation of neurons / spliceosomal complex assembly / monocyte differentiation / blastocyst development / neuron development / RHOBTB2 GTPase cycle / U6 snRNA binding / mRNA export from nucleus / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / RNA splicing / regulation of DNA-templated transcription elongation / central nervous system development / spliceosomal complex / cell morphogenesis / mRNA processing / nuclear matrix / mRNA splicing, via spliceosome / osteoblast differentiation / Signaling by CSF1 (M-CSF) in myeloid cells / negative regulation of neuron projection development / regulation of gene expression / RNA helicase activity / nuclear body / RNA helicase / nuclear speck / mRNA binding / apoptotic process / signal transduction / ATP hydrolysis activity / DNA binding / RNA binding / extracellular exosome / nucleoplasm / ATP binding / membrane / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
THO complex, subunit 5 / THO complex subunit 6 / Fms-interacting protein/Thoc5 / Chromatin target of PRMT1 protein, C-terminal / C-terminal duplication domain of Friend of PRMT1 / C-terminal duplication domain of Friend of PRMT1 / TREX component Tex1/THOC3 / THO complex subunit 7/Mft1 / THO complex, subunitTHOC2, C-terminal / THO complex, subunitTHOC2, N-terminal ...THO complex, subunit 5 / THO complex subunit 6 / Fms-interacting protein/Thoc5 / Chromatin target of PRMT1 protein, C-terminal / C-terminal duplication domain of Friend of PRMT1 / C-terminal duplication domain of Friend of PRMT1 / TREX component Tex1/THOC3 / 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 / WD40-like beta propeller / WD40-like Beta Propeller Repeat / Anaphase-promoting complex subunit 4, WD40 domain / Anaphase-promoting complex subunit 4 WD40 domain / Death domain profile. / DEATH domain, found in proteins involved in cell death (apoptosis). / Death domain / Death domain / RNA helicase, DEAD-box type, Q motif / DEAD-box RNA helicase Q motif profile. / Death-like domain superfamily / DEAD/DEAH box helicase / DEAD/DEAH box helicase domain / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / Helicase conserved C-terminal domain / RNA-binding domain superfamily / 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 / G-protein beta WD-40 repeat / Nucleotide-binding alpha-beta plait domain superfamily / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
THO complex subunit 5 homolog / Spliceosome RNA helicase DDX39B / THO complex subunit 7 homolog / THO complex subunit 4 / THO complex subunit 6 homolog / THO complex subunit 2 / THO complex subunit 1 / THO complex subunit 3
Similarity search - Component
Biological speciesHomo sapiens (human) / human (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.9 Å
AuthorsPacheco-Fiallos FB / Vorlaender MK / Plaschka C
Funding supportEuropean Union, 2 items
OrganizationGrant numberCountry
European Research Council (ERC)949081European Union
European Molecular Biology Organization (EMBO)623-2020European Union
CitationJournal: Nature / Year: 2023
Title: mRNA recognition and packaging by the human transcription-export complex.
Authors: Belén Pacheco-Fiallos / Matthias K Vorländer / Daria Riabov-Bassat / Laura Fin / Francis J O'Reilly / Farja I Ayala / Ulla Schellhaas / Juri Rappsilber / Clemens Plaschka /
Abstract: Newly made mRNAs are processed and packaged into mature ribonucleoprotein complexes (mRNPs) and are recognized by the essential transcription-export complex (TREX) for nuclear export. However, the ...Newly made mRNAs are processed and packaged into mature ribonucleoprotein complexes (mRNPs) and are recognized by the essential transcription-export complex (TREX) for nuclear export. However, the mechanisms of mRNP recognition and three-dimensional mRNP organization are poorly understood. Here we report cryo-electron microscopy and tomography structures of reconstituted and endogenous human mRNPs bound to the 2-MDa TREX complex. We show that mRNPs are recognized through multivalent interactions between the TREX subunit ALYREF and mRNP-bound exon junction complexes. Exon junction complexes can multimerize through ALYREF, which suggests a mechanism for mRNP organization. Endogenous mRNPs form compact globules that are coated by multiple TREX complexes. These results reveal how TREX may simultaneously recognize, compact and protect mRNAs to promote their packaging for nuclear export. The organization of mRNP globules provides a framework to understand how mRNP architecture facilitates mRNA biogenesis and export.
History
DepositionApr 21, 2022-
Header (metadata) releaseMay 3, 2023-
Map releaseMay 3, 2023-
UpdateMay 24, 2023-
Current statusMay 24, 2023Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_14804.png

Downloads & links

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Map

FileDownload / File: emd_14804.map.gz / Format: CCP4 / Size: 274.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationTREX-mRNA composite map generated from sharpened focused maps A (EMD 14805),B (EMD-14806) and C (EMD-14807 )
Voxel sizeX=Y=Z: 1.41 Å
Density
Contour LevelBy AUTHOR: 1.0
Minimum - Maximum0.0 - 11.951446
Average (Standard dev.)0.01431685 (±0.14560923)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions416416416
Spacing416416416
CellA=B=C: 586.56 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: TREX-mRNA composite map generated from unsharpened focused maps...

Fileemd_14804_additional_1.map
AnnotationTREX-mRNA composite map generated from unsharpened focused maps A (EMD 14805),B (EMD-14806) and C (EMD-14807
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : endogenous human TREX-mRNA complex

EntireName: endogenous human TREX-mRNA complex
Components
  • Complex: endogenous human TREX-mRNA complex
    • RNA: RNA
    • Protein or peptide: THO complex subunit 1
    • Protein or peptide: THO complex subunit 2
    • Protein or peptide: THO complex subunit 3
    • Protein or peptide: THO complex subunit 5 homolog
    • Protein or peptide: THO complex subunit 6 homolog
    • Protein or peptide: THO complex subunit 7 homolog
    • Protein or peptide: Spliceosome RNA helicase DDX39B
    • Protein or peptide: THO complex subunit 4

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Supramolecule #1: endogenous human TREX-mRNA complex

SupramoleculeName: endogenous human TREX-mRNA complex / type: complex / ID: 1 / Chimera: Yes / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 1.8 MDa

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Macromolecule #1: RNA

MacromoleculeName: RNA / type: rna / ID: 1 / Number of copies: 2
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 873.54 Da
SequenceString:
UUU

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Macromolecule #2: THO complex subunit 1

MacromoleculeName: THO complex subunit 1 / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: human (human)
Molecular weightTheoretical: 75.752156 KDa
SequenceString: MSPTPPLFSL PEARTRFTKS TREALNNKNI KPLLSTFSQV PGSENEKKCT LDQAFRGILE EEIINHSSCE NVLAIISLAI GGVTEGICT ASTPFVLLGD VLDCLPLDQC DTIFTFVEKN VATWKSNTFY SAGKNYLLRM CNDLLRRLSK SQNTVFCGRI Q LFLARLFP ...String:
MSPTPPLFSL PEARTRFTKS TREALNNKNI KPLLSTFSQV PGSENEKKCT LDQAFRGILE EEIINHSSCE NVLAIISLAI GGVTEGICT ASTPFVLLGD VLDCLPLDQC DTIFTFVEKN VATWKSNTFY SAGKNYLLRM CNDLLRRLSK SQNTVFCGRI Q LFLARLFP LSEKSGLNLQ SQFNLENVTV FNTNEQESTL GQKHTEDREE GMDVEEGEMG DEEAPTTCSI PIDYNLYRKF WS LQDYFRN PVQCYEKISW KTFLKYSEEV LAVFKSYKLD DTQASRKKME ELKTGGEHVY FAKFLTSEKL MDLQLSDSNF RRH ILLQYL ILFQYLKGQV KFKSSNYVLT DEQSLWIEDT TKSVYQLLSE NPPDGERFSK MVEHILNTEE NWNSWKNEGC PSFV KERTS DTKPTRIIRK RTAPEDFLGK GPTKKILMGN EELTRLWNLC PDNMEACKSE TREHMPTLEE FFEEAIEQAD PENMV ENEY KAVNNSNYGW RALRLLARRS PHFFQPTNQQ FKSLPEYLEN MVIKLAKELP PPSEEIKTGE DEDEEDNDAL LKENES PDV RRDKPVTGEQ IEVFANKLGE QWKILAPYLE MKDSEIRQIE CDSEDMKMRA KQLLVAWQDQ EGVHATPENL INALNKS GL SDLAESLTND NETNS

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Macromolecule #3: THO complex subunit 2

MacromoleculeName: THO complex subunit 2 / type: protein_or_peptide / ID: 3 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: human (human)
Molecular weightTheoretical: 183.087734 KDa
SequenceString: MAAAAVVVPA EWIKNWEKSG RGEFLHLCRI LSENKSHDSS TYRDFQQALY ELSYHVIKGN LKHEQASNVL SDISEFREDM PSILADVFC ILDIETNCLE EKSKRDYFTQ LVLACLYLVS DTVLKERLDP ETLESLGLIK QSQQFNQKSV KIKTKLFYKQ Q KFNLLREE ...String:
MAAAAVVVPA EWIKNWEKSG RGEFLHLCRI LSENKSHDSS TYRDFQQALY ELSYHVIKGN LKHEQASNVL SDISEFREDM PSILADVFC ILDIETNCLE EKSKRDYFTQ LVLACLYLVS DTVLKERLDP ETLESLGLIK QSQQFNQKSV KIKTKLFYKQ Q KFNLLREE NEGYAKLIAE LGQDLSGSIT SDLILENIKS LIGCFNLDPN RVLDVILEVF ECRPEHDDFF ISLLESYMSM CE PQTLCHI LGFKFKFYQE PNGETPSSLY RVAAVLLQFN LIDLDDLYVH LLPADNCIMD EHKREIAEAK QIVRKLTMVV LSS EKMDER EKEKEKEEEK VEKPPDNQKL GLLEALLKIG DWQHAQNIMD QMPPYYAASH KLIALAICKL IHITIEPLYR RVGV PKGAK GSPVNALQNK RAPKQAESFE DLRRDVFNMF CYLGPHLSHD PILFAKVVRI GKSFMKEFQS DGSKQEDKEK TEVIL SCLL SITDQVLLPS LSLMDCNACM SEELWGMFKT FPYQHRYRLY GQWKNETYNS HPLLVKVKAQ TIDRAKYIMK RLTKEN VKP SGRQIGKLSH SNPTILFDYI LSQIQKYDNL ITPVVDSLKY LTSLNYDVLA YCIIEALANP EKERMKHDDT TISSWLQ SL ASFCGAVFRK YPIDLAGLLQ YVANQLKAGK SFDLLILKEV VQKMAGIEIT EEMTMEQLEA MTGGEQLKAE GGYFGQIR N TKKSSQRLKD ALLDHDLALP LCLLMAQQRN GVIFQEGGEK HLKLVGKLYD QCHDTLVQFG GFLASNLSTE DYIKRVPSI DVLCNEFHTP HDAAFFLSRP MYAHHISSKY DELKKSEKGS KQQHKVHKYI TSCEMVMAPV HEAVVSLHVS KVWDDISPQF YATFWSLTM YDLAVPHTSY EREVNKLKVQ MKAIDDNQEM PPNKKKKEKE RCTALQDKLL EEEKKQMEHV QRVLQRLKLE K DNWLLAKS TKNETITKFL QLCIFPRCIF SAIDAVYCAR FVELVHQQKT PNFSTLLCYD RVFSDIIYTV ASCTENEASR YG RFLCCML ETVTRWHSDR ATYEKECGNY PGFLTILRAT GFDGGNKADQ LDYENFRHVV HKWHYKLTKA SVHCLETGEY THI RNILIV LTKILPWYPK VLNLGQALER RVHKICQEEK EKRPDLYALA MGYSGQLKSR KSYMIPENEF HHKDPPPRNA VASV QNGPG GGPSSSSIGS ASKSDESSTE ETDKSRERSQ CGVKAVNKAS STTPKGNSSN GNSGSNSNKA VKENDKEKGK EKEKE KKEK TPATTPEARV LGKDGKEKPK EERPNKDEKA RETKERTPKS DKEKEKFKKE EKAKDEKFKT TVPNAESKST QERERE KEP SRERDIAKEM KSKENVKGGE KTPVSGSLKS PVPRSDIPEP EREQKRRKID THPSPSHSST VKDSLIELKE SSAKLYI NH TPPPLSKSKE REMDKKDLDK SRERSREREK KDEKDRKERK RDHSNNDREV PPDLTKRRKE ENGTMGVSKH KSESPCES P YPNEKDKEKN KSKSSGKEKG SDSFKSEKMD KISSGGKKES RHDKEKIEKK EKRDSSGGKE EKKHHKSSDK HR

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Macromolecule #4: THO complex subunit 3

MacromoleculeName: THO complex subunit 3 / type: protein_or_peptide / ID: 4 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: human (human)
Molecular weightTheoretical: 38.817617 KDa
SequenceString: MAVPAAAMGP SALGQSGPGS MAPWCSVSSG PSRYVLGMQE LFRGHSKTRE FLAHSAKVHS VAWSCDGRRL ASGSFDKTAS VFLLEKDRL VKENNYRGHG DSVDQLCWHP SNPDLFVTAS GDKTIRIWDV RTTKCIATVN TKGENINICW SPDGQTIAVG N KDDVVTFI ...String:
MAVPAAAMGP SALGQSGPGS MAPWCSVSSG PSRYVLGMQE LFRGHSKTRE FLAHSAKVHS VAWSCDGRRL ASGSFDKTAS VFLLEKDRL VKENNYRGHG DSVDQLCWHP SNPDLFVTAS GDKTIRIWDV RTTKCIATVN TKGENINICW SPDGQTIAVG N KDDVVTFI DAKTHRSKAE EQFKFEVNEI SWNNDNNMFF LTNGNGCINI LSYPELKPVQ SINAHPSNCI CIKFDPMGKY FA TGSADAL VSLWDVDELV CVRCFSRLDW PVRTLSFSHD GKMLASASED HFIDIAEVET GDKLWEVQCE SPTFTVAWHP KRP LLAFAC DDKDGKYDSS REAGTVKLFG LPNDS

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Macromolecule #5: THO complex subunit 5 homolog

MacromoleculeName: THO complex subunit 5 homolog / type: protein_or_peptide / ID: 5 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: human (human)
Molecular weightTheoretical: 78.652898 KDa
SequenceString: MSSESSKKRK PKVIRSDGAP AEGKRNRSDT EQEGKYYSEE AEVDLRDPGR DYELYKYTCQ ELQRLMAEIQ DLKSRGGKDV AIEIEERRI QSCVHFMTLK KLNRLAHIRL KKGRDQTHEA KQKVDAYHLQ LQNLLYEVMH LQKEITKCLE FKSKHEEIDL V SLEEFYKE ...String:
MSSESSKKRK PKVIRSDGAP AEGKRNRSDT EQEGKYYSEE AEVDLRDPGR DYELYKYTCQ ELQRLMAEIQ DLKSRGGKDV AIEIEERRI QSCVHFMTLK KLNRLAHIRL KKGRDQTHEA KQKVDAYHLQ LQNLLYEVMH LQKEITKCLE FKSKHEEIDL V SLEEFYKE APPDISKAEV TMGDPHQQTL ARLDWELEQR KRLAEKYREC LSNKEKILKE IEVKKEYLSS LQPRLNSIMQ AS LPVQEYL FMPFDQAHKQ YETARHLPPP LYVLFVQATA YGQACDKTLS VAIEGSVDEA KALFKPPEDS QDDESDSDAE EEQ TTKRRR PTLGVQLDDK RKEMLKRHPL SVMLDLKCKD DSVLHLTFYY LMNLNIMTVK AKVTTAMELI TPISAGDLLS PDSV LSCLY PGDHGKKTPN PANQYQFDKV GILTLSDYVL ELGHPYLWVQ KLGGLHFPKE QPQQTVIADH SLSASHMETT MKLLK TRVQ SRLALHKQFA SLEHGIVPVT SDCQYLFPAK VVSRLVKWVT IAHEDYMELH FTKDIVDAGL AGDTNLYYMA LIERGT AKL QAAVVLNPGY SSIPPIFQLC LNWKGEKTNS NDDNIRAMEG EVNVCYKELC GPWPSHQLLT NQLQRLCVLL DVYLETE SH DDSVEGPKEF PQEKMCLRLF RGPSRMKPFK YNHPQGFFSH R

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Macromolecule #6: THO complex subunit 6 homolog

MacromoleculeName: THO complex subunit 6 homolog / type: protein_or_peptide / ID: 6 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: human (human)
Molecular weightTheoretical: 37.577875 KDa
SequenceString: MERAVPLAVP LGQTEVFQAL QRLHMTIFSQ SVSPCGKFLA AGNNYGQIAI FSLSSALSSE AKEESKKPVV TFQAHDGPVY SMVSTDRHL LSAGDGEVKA WLWAEMLKKG CKELWRRQPP YRTSLEVPEI NALLLVPKEN SLILAGGDCQ LHTMDLETGT F TRVLRGHT ...String:
MERAVPLAVP LGQTEVFQAL QRLHMTIFSQ SVSPCGKFLA AGNNYGQIAI FSLSSALSSE AKEESKKPVV TFQAHDGPVY SMVSTDRHL LSAGDGEVKA WLWAEMLKKG CKELWRRQPP YRTSLEVPEI NALLLVPKEN SLILAGGDCQ LHTMDLETGT F TRVLRGHT DYIHCLALRE RSPEVLSGGE DGAVRLWDLR TAKEVQTIEV YKHEECSRPH NGRWIGCLAT DSDWMVCGGG PA LTLWHLR SSTPTTIFPI RAPQKHVTFY QDLILSAGQG RCVNQWQLSG ELKAQVPGSS PGLLSLSLNQ QPAAPECKVL TAA GNSCRV DVFTNLGYRA FSLSF

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Macromolecule #7: THO complex subunit 7 homolog

MacromoleculeName: THO complex subunit 7 homolog / type: protein_or_peptide / ID: 7 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: human (human)
Molecular weightTheoretical: 23.782014 KDa
SequenceString: MGAVTDDEVI RKRLLIDGDG AGDDRRINLL VKSFIKWCNS GSQEEGYSQY QRMLSTLSQC EFSMGKTLLV YDMNLREMEN YEKIYKEIE CSIAGAHEKI AECKKQILQA KRIRKNRQEY DALAKVIQHH PDRHETLKEL EALGKELEHL SHIKESVEDK L ELRRKQFH ...String:
MGAVTDDEVI RKRLLIDGDG AGDDRRINLL VKSFIKWCNS GSQEEGYSQY QRMLSTLSQC EFSMGKTLLV YDMNLREMEN YEKIYKEIE CSIAGAHEKI AECKKQILQA KRIRKNRQEY DALAKVIQHH PDRHETLKEL EALGKELEHL SHIKESVEDK L ELRRKQFH VLLSTIHELQ QTLENDEKLS EVEEAQEASM ETDPKP

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Macromolecule #8: Spliceosome RNA helicase DDX39B

MacromoleculeName: Spliceosome RNA helicase DDX39B / type: protein_or_peptide / ID: 8 / Number of copies: 4 / Enantiomer: LEVO / EC number: RNA helicase
Source (natural)Organism: human (human)
Molecular weightTheoretical: 49.05625 KDa
SequenceString: MAENDVDNEL LDYEDDEVET AAGGDGAEAP AKKDVKGSYV SIHSSGFRDF LLKPELLRAI VDCGFEHPSE VQHECIPQAI LGMDVLCQA KSGMGKTAVF VLATLQQLEP VTGQVSVLVM CHTRELAFQI SKEYERFSKY MPNVKVAVFF GGLSIKKDEE V LKKNCPHI ...String:
MAENDVDNEL LDYEDDEVET AAGGDGAEAP AKKDVKGSYV SIHSSGFRDF LLKPELLRAI VDCGFEHPSE VQHECIPQAI LGMDVLCQA KSGMGKTAVF VLATLQQLEP VTGQVSVLVM CHTRELAFQI SKEYERFSKY MPNVKVAVFF GGLSIKKDEE V LKKNCPHI VVGTPGRILA LARNKSLNLK HIKHFILDEC DKMLEQLDMR RDVQEIFRMT PHEKQVMMFS ATLSKEIRPV CR KFMQDPM EIFVDDETKL TLHGLQQYYV KLKDNEKNRK LFDLLDVLEF NQVVIFVKSV QRCIALAQLL VEQNFPAIAI HRG MPQEER LSRYQQFKDF QRRILVATNL FGRGMDIERV NIAFNYDMPE DSDTYLHRVA RAGRFGTKGL AITFVSDEND AKIL NDVQD RFEVNISELP DEIDISSYIE QTR

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Macromolecule #9: THO complex subunit 4

MacromoleculeName: THO complex subunit 4 / type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: human (human)
Molecular weightTheoretical: 26.934002 KDa
SequenceString: MADKMDMSLD DIIKLNRSQR GGRGGGRGRG RAGSQGGRGG GAQAAARVNR GGGPIRNRPA IARGAAGGGG RNRPAPYSRP KQLPDKWQH DLFDSGFGGG AGVETGGKLL VSNLDFGVSD ADIQELFAEF GTLKKAAVHY DRSGRSLGTA DVHFERKADA L KAMKQYNG ...String:
MADKMDMSLD DIIKLNRSQR GGRGGGRGRG RAGSQGGRGG GAQAAARVNR GGGPIRNRPA IARGAAGGGG RNRPAPYSRP KQLPDKWQH DLFDSGFGGG AGVETGGKLL VSNLDFGVSD ADIQELFAEF GTLKKAAVHY DRSGRSLGTA DVHFERKADA L KAMKQYNG VPLDGRPMNI QLVTSQIDAQ RRPAQSVNRG GMTRNRGAGG FGGGGGTRRG TRGGARGRGR GAGRNSKQQL SA EELDAQL DAYNARMDTS

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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

Concentration0.2 mg/mL
BufferpH: 7.9
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 / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.5 µm
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: EMDB MAP
EMDB ID:

11857

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 182534

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