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- EMDB-10772: Structure of a human 48S translational initiation complex - head -

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Basic information

Entry
Database: EMDB / ID: EMD-10772
TitleStructure of a human 48S translational initiation complex - head
Map data
Sample
  • Complex: 48S initiation complex
    • Protein or peptide: x 17 types
    • RNA: x 1 types
  • Ligand: x 2 types
Keywordsribosome / translation / initiation complex
Function / homology
Function and homology information


positive regulation of mRNA binding / viral translational termination-reinitiation / cap-dependent translational initiation / eukaryotic translation initiation factor 3 complex, eIF3m / IRES-dependent viral translational initiation / eukaryotic translation initiation factor 3 complex / formation of cytoplasmic translation initiation complex / eukaryotic 43S preinitiation complex / mRNA cap binding / eukaryotic 48S preinitiation complex ...positive regulation of mRNA binding / viral translational termination-reinitiation / cap-dependent translational initiation / eukaryotic translation initiation factor 3 complex, eIF3m / IRES-dependent viral translational initiation / eukaryotic translation initiation factor 3 complex / formation of cytoplasmic translation initiation complex / eukaryotic 43S preinitiation complex / mRNA cap binding / eukaryotic 48S preinitiation complex / negative regulation of endoplasmic reticulum unfolded protein response / oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / negative regulation of peptidyl-serine phosphorylation / positive regulation of respiratory burst involved in inflammatory response / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / positive regulation of gastrulation / regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / protein tyrosine kinase inhibitor activity / IRE1-RACK1-PP2A complex / positive regulation of endodeoxyribonuclease activity / nucleolus organization / positive regulation of Golgi to plasma membrane protein transport / TNFR1-mediated ceramide production / negative regulation of DNA repair / supercoiled DNA binding / NF-kappaB complex / oxidized purine DNA binding / cysteine-type endopeptidase activator activity involved in apoptotic process / negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide / ubiquitin-like protein conjugating enzyme binding / regulation of establishment of cell polarity / Formation of the ternary complex, and subsequently, the 43S complex / negative regulation of phagocytosis / erythrocyte homeostasis / cytoplasmic side of rough endoplasmic reticulum membrane / protein kinase A binding / pigmentation / Ribosomal scanning and start codon recognition / ion channel inhibitor activity / Translation initiation complex formation / positive regulation of mitochondrial depolarization / positive regulation of T cell receptor signaling pathway / positive regulation of activated T cell proliferation / fibroblast growth factor binding / negative regulation of Wnt signaling pathway / monocyte chemotaxis / negative regulation of translational frameshifting / BH3 domain binding / SARS-CoV-1 modulates host translation machinery / regulation of cell division / Peptide chain elongation / iron-sulfur cluster binding / Selenocysteine synthesis / positive regulation of signal transduction by p53 class mediator / Formation of a pool of free 40S subunits / ubiquitin ligase inhibitor activity / Eukaryotic Translation Termination / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / Viral mRNA Translation / negative regulation of respiratory burst involved in inflammatory response / phagocytic cup / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / regulation of translational fidelity / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / spindle assembly / ribosomal small subunit export from nucleus / positive regulation of intrinsic apoptotic signaling pathway / translation regulator activity / signaling adaptor activity / gastrulation / Maturation of protein E / Maturation of protein E / MDM2/MDM4 family protein binding / positive regulation of microtubule polymerization / cytosolic ribosome / ER Quality Control Compartment (ERQC) / DNA-(apurinic or apyrimidinic site) endonuclease activity / rescue of stalled ribosome / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / translation initiation factor activity / negative regulation of protein binding / negative regulation of protein ubiquitination / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / positive regulation of GTPase activity / Membrane binding and targetting of GAG proteins / Endosomal Sorting Complex Required For Transport (ESCRT) / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / Negative regulation of FLT3
Similarity search - Function
Eukaryotic translation initiation factor 3 subunit D / Eukaryotic translation initiation factor 3 subunit 7 (eIF-3) / Eukaryotic translation initiation factor 3 subunit G / Eukaryotic translation initiation factor 3 subunit G, N-terminal / eIF3G, RNA recognition motif / Eukaryotic translation initiation factor 3 subunit G / : / Ribosomal protein S12e signature. / Ribosomal protein S12e / Ribosomal protein S19e, conserved site ...Eukaryotic translation initiation factor 3 subunit D / Eukaryotic translation initiation factor 3 subunit 7 (eIF-3) / Eukaryotic translation initiation factor 3 subunit G / Eukaryotic translation initiation factor 3 subunit G, N-terminal / eIF3G, RNA recognition motif / Eukaryotic translation initiation factor 3 subunit G / : / Ribosomal protein S12e signature. / Ribosomal protein S12e / Ribosomal protein S19e, conserved site / Ribosomal protein S19e signature. / Small (40S) ribosomal subunit Asc1/RACK1 / S27a-like superfamily / 40S Ribosomal protein S10 / Plectin/S10, N-terminal / Plectin/S10 domain / Ribosomal protein S10, eukaryotic/archaeal / Ribosomal protein S25 / S25 ribosomal protein / Ribosomal protein S27a / Ribosomal protein S17e, conserved site / Ribosomal protein S27a / Ribosomal protein S17e signature. / Ribosomal protein S27a / 40S ribosomal protein S29/30S ribosomal protein S14 type Z / Ribosomal protein S3, eukaryotic/archaeal / Ribosomal protein S19e / Ribosomal protein S19e / Ribosomal_S19e / Ribosomal protein S19A/S15e / Ribosomal protein S17e / Ribosomal protein S17e-like superfamily / Ribosomal S17 / Ribosomal protein S28e conserved site / Ribosomal protein S28e signature. / Ribosomal protein S28e / Ribosomal protein S28e / Ribosomal protein S5/S7, eukaryotic/archaeal / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / Ribosomal protein S14/S29 / Ribosomal protein L7Ae/L30e/S12e/Gadd45 / Ribosomal protein L7Ae/L30e/S12e/Gadd45 family / RNA-binding domain superfamily / 50S ribosomal protein L30e-like / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ribosomal protein S3, conserved site / Ribosomal protein S3 signature. / Ribosomal protein S10, conserved site / Ribosomal protein S10 signature. / Ribosomal protein S14, conserved site / Ribosomal protein S14 signature. / KH domain / Type-2 KH domain profile. / K Homology domain, type 2 / Ribosomal protein S3, C-terminal / Ribosomal protein S3, C-terminal domain / Ribosomal protein S3, C-terminal domain superfamily / Ribosomal protein S15/S19, conserved site / Ribosomal protein S19 signature. / Ribosomal protein S10 / Ribosomal protein S19/S15 / Ribosomal protein S19/S15, superfamily / Ribosomal protein S19 / Ribosomal protein S7, conserved site / Ribosomal protein S7 signature. / Ubiquitin family / K homology domain superfamily, prokaryotic type / Ribosomal protein S13, conserved site / Ribosomal protein S13 signature. / Ribosomal protein S13 / 30s ribosomal protein S13, C-terminal / Ribosomal protein S13/S18 / Ribosomal protein S13 family profile. / Ribosomal protein S14 / Ribosomal protein S14p/S29e / K homology domain-like, alpha/beta / Ubiquitin homologues / Ribosomal protein S13-like, H2TH / Ribosomal protein S10p/S20e / Ribosomal protein S9, conserved site / Ribosomal protein S9 signature. / Ribosomal protein S10 domain / Ribosomal protein S10 domain superfamily / Ribosomal protein S10p/S20e / Ubiquitin domain profile. / Ribosomal protein S5/S7 / Ribosomal protein S7 domain / Ribosomal protein S7 domain superfamily / Ribosomal protein S7p/S5e / Ubiquitin-like domain / Ribosomal protein S9 / Ribosomal protein S9/S16 / Zinc-binding ribosomal protein / Ribosomal protein S5 domain 2-type fold, subgroup
Similarity search - Domain/homology
Eukaryotic translation initiation factor 3 subunit D / Eukaryotic translation initiation factor 3 subunit G / Small ribosomal subunit protein eS17 / Small ribosomal subunit protein uS3 / Small ribosomal subunit protein eS12 / Small ribosomal subunit protein eS19 / Small ribosomal subunit protein uS7 / Small ribosomal subunit protein eS10 / Small ribosomal subunit protein uS10 / Small ribosomal subunit protein uS9 ...Eukaryotic translation initiation factor 3 subunit D / Eukaryotic translation initiation factor 3 subunit G / Small ribosomal subunit protein eS17 / Small ribosomal subunit protein uS3 / Small ribosomal subunit protein eS12 / Small ribosomal subunit protein eS19 / Small ribosomal subunit protein uS7 / Small ribosomal subunit protein eS10 / Small ribosomal subunit protein uS10 / Small ribosomal subunit protein uS9 / Small ribosomal subunit protein uS13 / Small ribosomal subunit protein uS14 / Small ribosomal subunit protein uS19 / Small ribosomal subunit protein eS25 / Small ribosomal subunit protein eS28 / Ubiquitin-ribosomal protein eS31 fusion protein / Small ribosomal subunit protein RACK1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsBrito Querido J / Sokabe M
Funding support United Kingdom, United States, 3 items
OrganizationGrant numberCountry
Wellcome TrustWTY096570 United Kingdom
Medical Research Council (MRC, United Kingdom)MC_U105184332 United Kingdom
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM092927 United States
CitationJournal: Science / Year: 2020
Title: Structure of a human 48 translational initiation complex.
Authors: Jailson Brito Querido / Masaaki Sokabe / Sebastian Kraatz / Yuliya Gordiyenko / J Mark Skehel / Christopher S Fraser / V Ramakrishnan /
Abstract: A key step in translational initiation is the recruitment of the 43 preinitiation complex by the cap-binding complex [eukaryotic initiation factor 4F (eIF4F)] at the 5' end of messenger RNA (mRNA) to ...A key step in translational initiation is the recruitment of the 43 preinitiation complex by the cap-binding complex [eukaryotic initiation factor 4F (eIF4F)] at the 5' end of messenger RNA (mRNA) to form the 48 initiation complex (i.e., the 48). The 48 then scans along the mRNA to locate a start codon. To understand the mechanisms involved, we used cryo-electron microscopy to determine the structure of a reconstituted human 48 The structure reveals insights into early events of translation initiation complex assembly, as well as how eIF4F interacts with subunits of eIF3 near the mRNA exit channel in the 43 The location of eIF4F is consistent with a slotting model of mRNA recruitment and suggests that downstream mRNA is unwound at least in part by being "pulled" through the 40 subunit during scanning.
History
DepositionMar 17, 2020-
Header (metadata) releaseSep 16, 2020-
Map releaseSep 16, 2020-
UpdateApr 24, 2024-
Current statusApr 24, 2024Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.033
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  • Surface view colored by height
  • Surface level: 0.033
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  • Surface view with fitted model
  • Atomic models: PDB-6ybs
  • Surface level: 0.033
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6ybs
  • Imaged by Jmol
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Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_10772.png

Downloads & links

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Map

FileDownload / File: emd_10772.map.gz / Format: CCP4 / Size: 476.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 500 pix.
= 537. Å		1.07 Å/pix.
x 500 pix.
= 537. Å		1.07 Å/pix.
x 500 pix.
= 537. Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.074 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.02 / Movie #1: 0.033
Minimum - Maximum-0.20110273 - 0.40833396
Average (Standard dev.)0.00013005463 (±0.004569401)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions500500500
Spacing500500500
CellA=B=C: 537.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0741.0741.074
M x/y/z500500500
origin x/y/z0.0000.0000.000
length x/y/z537.000537.000537.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS500500500
D min/max/mean-0.2010.4080.000

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Supplemental data

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Mask #1

Fileemd_10772_msk_1.map
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Additional map: #1

Fileemd_10772_additional_1.map
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Additional map: #2

Fileemd_10772_additional_2.map
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Half map: #1

Fileemd_10772_half_map_1.map
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Half map: #2

Fileemd_10772_half_map_2.map
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Sample components

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Entire : 48S initiation complex

EntireName: 48S initiation complex
Components
  • Complex: 48S initiation complex
    • Protein or peptide: Eukaryotic translation initiation factor 3 subunit D
    • Protein or peptide: Receptor of activated protein C kinase 1
    • Protein or peptide: 40S ribosomal protein S28
    • Protein or peptide: 40S ribosomal protein S17
    • Protein or peptide: 40S ribosomal protein S20
    • Protein or peptide: Eukaryotic translation initiation factor 3 subunit G
    • Protein or peptide: 40S ribosomal protein S10
    • Protein or peptide: 40S ribosomal protein S12
    • Protein or peptide: 40S ribosomal protein S29
    • Protein or peptide: 40S ribosomal protein S15
    • Protein or peptide: 40S ribosomal protein S3
    • Protein or peptide: 40S ribosomal protein S19
    • Protein or peptide: 40S ribosomal protein S25
    • Protein or peptide: 40S ribosomal protein S18
    • Protein or peptide: 40S ribosomal protein S5
    • Protein or peptide: Ubiquitin-40S ribosomal protein S27a
    • Protein or peptide: 40S ribosomal protein S16
    • RNA: 18S rRNA
  • Ligand: MAGNESIUM ION
  • Ligand: ZINC ION

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Supramolecule #1: 48S initiation complex

SupramoleculeName: 48S initiation complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#18
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Eukaryotic translation initiation factor 3 subunit D

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit D / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 64.060758 KDa
SequenceString: MAKFMTPVIQ DNPSGWGPCA VPEQFRDMPY QPFSKGDRLG KVADWTGATY QDKRYTNKYS SQFGGGSQYA YFHEEDESSF QLVDTARTQ KTAYQRNRMR FAQRNLRRDK DRRNMLQFNL QILPKSAKQK ERERIRLQKK FQKQFGVRQK WDQKSQKPRD S SVEVRSDW ...String:
MAKFMTPVIQ DNPSGWGPCA VPEQFRDMPY QPFSKGDRLG KVADWTGATY QDKRYTNKYS SQFGGGSQYA YFHEEDESSF QLVDTARTQ KTAYQRNRMR FAQRNLRRDK DRRNMLQFNL QILPKSAKQK ERERIRLQKK FQKQFGVRQK WDQKSQKPRD S SVEVRSDW EVKEEMDFPQ LMKMRYLEVS EPQDIECCGA LEYYDKAFDR ITTRSEKPLR SIKRIFHTVT TTDDPVIRKL AK TQGNVFA TDAILATLMS CTRSVYSWDI VVQRVGSKLF FDKRDNSDFD LLTVSETANE PPQDEGNSFN SPRNLAMEAT YIN HNFSQQ CLRMGKERYN FPNPNPFVED DMDKNEIASV AYRYRRWKLG DDIDLIVRCE HDGVMTGANG EVSFINIKTL NEWD SRHCN GVDWRQKLDS QRGAVIATEL KNNSYKLARW TCCALLAGSE YLKLGYVSRY HVKDSSRHVI LGTQQFKPNE FASQI NLSV ENAWGILRCV IDICMKLEEG KYLILKDPNK QVIRVYSLPD GTFSSDEDEE EEEEEEEEEE EEET

UniProtKB: Eukaryotic translation initiation factor 3 subunit D

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Macromolecule #2: Receptor of activated protein C kinase 1

MacromoleculeName: Receptor of activated protein C kinase 1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 35.115652 KDa
SequenceString: MTEQMTLRGT LKGHNGWVTQ IATTPQFPDM ILSASRDKTI IMWKLTRDET NYGIPQRALR GHSHFVSDVV ISSDGQFALS GSWDGTLRL WDLTTGTTTR RFVGHTKDVL SVAFSSDNRQ IVSGSRDKTI KLWNTLGVCK YTVQDESHSE WVSCVRFSPN S SNPIIVSC ...String:
MTEQMTLRGT LKGHNGWVTQ IATTPQFPDM ILSASRDKTI IMWKLTRDET NYGIPQRALR GHSHFVSDVV ISSDGQFALS GSWDGTLRL WDLTTGTTTR RFVGHTKDVL SVAFSSDNRQ IVSGSRDKTI KLWNTLGVCK YTVQDESHSE WVSCVRFSPN S SNPIIVSC GWDKLVKVWN LANCKLKTNH IGHTGYLNTV TVSPDGSLCA SGGKDGQAML WDLNEGKHLY TLDGGDIINA LC FSPNRYW LCAATGPSIK IWDLEGKIIV DELKQEVIST SSKAEPPQCT SLAWSADGQT LFAGYTDNLV RVWQVTIGTR

UniProtKB: Small ribosomal subunit protein RACK1

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Macromolecule #3: 40S ribosomal protein S28

MacromoleculeName: 40S ribosomal protein S28 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 7.855052 KDa
SequenceString:
MDTSRVQPIK LARVTKVLGR TGSQGQCTQV RVEFMDDTSR SIIRNVKGPV REGDVLTLLE SEREARRLR

UniProtKB: Small ribosomal subunit protein eS28

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Macromolecule #4: 40S ribosomal protein S17

MacromoleculeName: 40S ribosomal protein S17 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.578156 KDa
SequenceString:
MGRVRTKTVK KAARVIIEKY YTRLGNDFHT NKRVCEEIAI IPSKKLRNKI AGYVTHLMKR IQRGPVRGIS IKLQEEERER RDNYVPEVS ALDQEIIEVD PDTKEMLKLL DFGSLSNLQV TQPTVGMNFK TPRGPV

UniProtKB: Small ribosomal subunit protein eS17

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Macromolecule #5: 40S ribosomal protein S20

MacromoleculeName: 40S ribosomal protein S20 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.398763 KDa
SequenceString:
MAFKDTGKTP VEPEVAIHRI RITLTSRNVK SLEKVCADLI RGAKEKNLKV KGPVRMPTKT LRITTRKTPC GEGSKTWDRF QMRIHKRLI DLHSPSEIVK QITSISIEPG VEVEVTIADA

UniProtKB: Small ribosomal subunit protein uS10

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Macromolecule #6: Eukaryotic translation initiation factor 3 subunit G

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit G / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 35.662016 KDa
SequenceString: MPTGDFDSKP SWADQVEEEG EDDKCVTSEL LKGIPLATGD TSPEPELLPG APLPPPKEVI NGNIKTVTEY KIDEDGKKFK IVRTFRIET RKASKAVARR KNWKKFGNSE FDPPGPNVAT TTVSDDVSMT FITSKEDLNC QEEEDPMNKL KGQKIVSCRI C KGDHWTTR ...String:
MPTGDFDSKP SWADQVEEEG EDDKCVTSEL LKGIPLATGD TSPEPELLPG APLPPPKEVI NGNIKTVTEY KIDEDGKKFK IVRTFRIET RKASKAVARR KNWKKFGNSE FDPPGPNVAT TTVSDDVSMT FITSKEDLNC QEEEDPMNKL KGQKIVSCRI C KGDHWTTR CPYKDTLGPM QKELAEQLGL STGEKEKLPG ELEPVQATQN KTGKYVPPSL RDGASRRGES MQPNRRADDN AT IRVTNLS EDTRETDLQE LFRPFGSISR IYLAKDKTTG QSKGFAFISF HRREDAARAI AGVSGFGYDH LILNVEWAKP STN

UniProtKB: Eukaryotic translation initiation factor 3 subunit G

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Macromolecule #7: 40S ribosomal protein S10

MacromoleculeName: 40S ribosomal protein S10 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 18.933846 KDa
SequenceString:
MLMPKKNRIA IYELLFKEGV MVAKKDVHMP KHPELADKNV PNLHVMKAMQ SLKSRGYVKE QFAWRHFYWY LTNEGIQYLR DYLHLPPEI VPATLRRSRP ETGRPRPKGL EGERPARLTR GEADRDTYRR SAVPPGADKK AEAGAGSATE FQFRGGFGRG R GQPPQ

UniProtKB: Small ribosomal subunit protein eS10

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Macromolecule #8: 40S ribosomal protein S12

MacromoleculeName: 40S ribosomal protein S12 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.538987 KDa
SequenceString:
MAEEGIAAGG VMDVNTALQE VLKTALIHDG LARGIREAAK ALDKRQAHLC VLASNCDEPM YVKLVEALCA EHQINLIKVD DNKKLGEWV GLCKIDREGK PRKVVGCSCV VVKDYGKESQ AKDVIEEYFK CKK

UniProtKB: Small ribosomal subunit protein eS12

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Macromolecule #9: 40S ribosomal protein S29

MacromoleculeName: 40S ribosomal protein S29 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 6.690821 KDa
SequenceString:
MGHQQLYWSH PRKFGQGSRS CRVCSNRHGL IRKYGLNMCR QCFRQYAKDI GFIKLD

UniProtKB: Small ribosomal subunit protein uS14

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Macromolecule #10: 40S ribosomal protein S15

MacromoleculeName: 40S ribosomal protein S15 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 17.076207 KDa
SequenceString:
MAEVEQKKKR TFRKFTYRGV DLDQLLDMSY EQLMQLYSAR QRRRLNRGLR RKQHSLLKRL RKAKKEAPPM EKPEVVKTHL RDMIILPEM VGSMVGVYNG KTFNQVEIKP EMIGHYLGEF SITYKPVKHG RPGIGATHSS RFIPLK

UniProtKB: Small ribosomal subunit protein uS19

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Macromolecule #11: 40S ribosomal protein S3

MacromoleculeName: 40S ribosomal protein S3 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-(apurinic or apyrimidinic site) lyase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 26.729369 KDa
SequenceString: MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII LATRTQNVLG EKGRRIRELT AVVQKRFGFP EGSVELYAE KVATRGLCAI AQAESLRYKL LGGLAVRRAC YGVLRFIMES GAKGCEVVVS GKLRGQRAKS MKFVDGLMIH S GDPVNYYV ...String:
MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII LATRTQNVLG EKGRRIRELT AVVQKRFGFP EGSVELYAE KVATRGLCAI AQAESLRYKL LGGLAVRRAC YGVLRFIMES GAKGCEVVVS GKLRGQRAKS MKFVDGLMIH S GDPVNYYV DTAVRHVLLR QGVLGIKVKI MLPWDPTGKI GPKKPLPDHV SIVEPKDEIL PTTPISEQKG GKPEPPAMPQ PV PTA

UniProtKB: Small ribosomal subunit protein uS3

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Macromolecule #12: 40S ribosomal protein S19

MacromoleculeName: 40S ribosomal protein S19 / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 16.091562 KDa
SequenceString:
MPGVTVKDVN QQEFVRALAA FLKKSGKLKV PEWVDTVKLA KHKELAPYDE NWFYTRAAST ARHLYLRGGA GVGSMTKIYG GRQRNGVMP SHFSRGSKSV ARRVLQALEG LKMVEKDQDG GRKLTPQGQR DLDRIAGQVA AANKKH

UniProtKB: Small ribosomal subunit protein eS19

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Macromolecule #13: 40S ribosomal protein S25

MacromoleculeName: 40S ribosomal protein S25 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.776224 KDa
SequenceString:
MPPKDDKKKK DAGKSAKKDK DPVNKSGGKA KKKKWSKGKV RDKLNNLVLF DKATYDKLCK EVPNYKLITP AVVSERLKIR GSLARAALQ ELLSKGLIKL VSKHRAQVIY TRNTKGGDAP AAGEDA

UniProtKB: Small ribosomal subunit protein eS25

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Macromolecule #14: 40S ribosomal protein S18

MacromoleculeName: 40S ribosomal protein S18 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 17.759777 KDa
SequenceString:
MSLVIPEKFQ HILRVLNTNI DGRRKIAFAI TAIKGVGRRY AHVVLRKADI DLTKRAGELT EDEVERVITI MQNPRQYKIP DWFLNRQKD VKDGKYSQVL ANGLDNKLRE DLERLKKIRA HRGLRHFWGL RVRGQHTKTT GRRGRTVGVS KKK

UniProtKB: Small ribosomal subunit protein uS13

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Macromolecule #15: 40S ribosomal protein S5

MacromoleculeName: 40S ribosomal protein S5 / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 22.913453 KDa
SequenceString: MTEWETAAPA VAETPDIKLF GKWSTDDVQI NDISLQDYIA VKEKYAKYLP HSAGRYAAKR FRKAQCPIVE RLTNSMMMHG RNNGKKLMT VRIVKHAFEI IHLLTGENPL QVLVNAIINS GPREDSTRIG RAGTVRRQAV DVSPLRRVNQ AIWLLCTGAR E AAFRNIKT ...String:
MTEWETAAPA VAETPDIKLF GKWSTDDVQI NDISLQDYIA VKEKYAKYLP HSAGRYAAKR FRKAQCPIVE RLTNSMMMHG RNNGKKLMT VRIVKHAFEI IHLLTGENPL QVLVNAIINS GPREDSTRIG RAGTVRRQAV DVSPLRRVNQ AIWLLCTGAR E AAFRNIKT IAECLADELI NAAKGSSNSY AIKKKDELER VAKSNR

UniProtKB: Small ribosomal subunit protein uS7

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Macromolecule #16: Ubiquitin-40S ribosomal protein S27a

MacromoleculeName: Ubiquitin-40S ribosomal protein S27a / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 18.004041 KDa
SequenceString:
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGGAKKR KKKSYTTPK KNKHKRKKVK LAVLKYYKVD ENGKISRLRR ECPSDECGAG VFMASHFDRH YCGKCCLTYC FNKPEDK

UniProtKB: Ubiquitin-ribosomal protein eS31 fusion protein

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Macromolecule #17: 40S ribosomal protein S16

MacromoleculeName: 40S ribosomal protein S16 / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 16.477377 KDa
SequenceString:
MPSKGPLQSV QVFGRKKTAT AVAHCKRGNG LIKVNGRPLE MIEPRTLQYK LLEPVLLLGK ERFAGVDIRV RVKGGGHVAQ IYAIRQSIS KALVAYYQKY VDEASKKEIK DILIQYDRTL LVADPRRCES KKFGGPGARA RYQKSYR

UniProtKB: Small ribosomal subunit protein uS9

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Macromolecule #18: 18S rRNA

MacromoleculeName: 18S rRNA / type: rna / ID: 18 / Number of copies: 1
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 603.130375 KDa
SequenceString: UACCUGGUUG AUCCUGCCAG UAGCAU(A2M)UGC UUGUCUCAAA GAUUAAGCCA UGCAUGUCUG AGUACGCACG GCCGGU ACA GUGAAACUGC GAAUGGCUCA UUAAAUCAGU UAUGGU(OMU)CC(PSU) U(OMU)GGUCGCUC GCUCCUCUCC UACUU GGAU AACUGUGGUA ...String:
UACCUGGUUG AUCCUGCCAG UAGCAU(A2M)UGC UUGUCUCAAA GAUUAAGCCA UGCAUGUCUG AGUACGCACG GCCGGU ACA GUGAAACUGC GAAUGGCUCA UUAAAUCAGU UAUGGU(OMU)CC(PSU) U(OMU)GGUCGCUC GCUCCUCUCC UACUU GGAU AACUGUGGUA (A2M)UUCUAG(A2M)GC UAAUA(OMC)AUGC CGACGGGCGC UGACCCCCUU CGCGGGGGGG AUGC GUGCA UUUAUCAGAU CAAAACCAAC CCGGUCAGCC CCUCUCCGGC CCCGGCCGGG GGGCGGGCGC CGGCGGCUUU GGUGA CUCU AGAUAACCUC GGGCCGAUCG CACGCCCCCC GUGGCGGCGA CGACCCAUUC GAACGUCUGC CCUAUCAACU UUCGAU GGU AGUCGCCGUG CCUACCAUGG UGACCACGGG UGACGGGGAA UCAGGGUUCG AUUCCGGAGA GGGAGCCUGA GAAACGG CU ACCACAUCCA AGGAAGGCAG CAGGCGCGC(A2M) AAUUACCCAC UCCCGACCCG GGGA(OMG)GUAGU GA(OMC)GAA AAA UAACAAUACA GGACUCUUUC GAGGCCCUGU AAUUGGAAUG AGUCCACUUU AAAUCCUUUA ACGAGGAUCC AUUGGAG GG CAAGUCUGG(PSU) GCCAGCAGCC GCGGUAAUUC CAGCUCCAAU A(OMG)CGUAUAUU AAAGUUGCUG CAGUU(A2M) AAA AGCUCGUAGU U(OMG)GAUCUUGG GAGCGGGCGG GCGGUCCGCC GCGAGGCGAG CCACCGCCCG UCCCCGCCCC UUG CCUCUC GGCGCCCCCU CGAUGCUCUU AGCUGAGUGU CCCGCGGGGC CCGAAGCGUU UACUUUGAAA AAA(5MU)UAGAGU G(PSU)(PSU)CAAAGC AGGCCCGAGC CGCCUGGAUA CCGCAGCUAG GAAUAAUGGA AUAGGACCGC GGUUCUAUUU UGU UGGUUU UCGGAACUGA GGCCAUGAUU AAGAGGGACG GCCGGGGGCA UUCGUAUUGC GCCGCUAGAG GUGAAAUUCU UGGA CCGGC GCAAGACGGA CCAGAGCGAA AGCAUUUGCC AAGAAUGUUU UCAUUAAUCA AGA(A2M)CGAAAG UCGGAGGUUC G AAGACGAU CAGAUACCGU CGUAGUUCCG ACCA(PSU)AAACG AUGCCGACCG GCGAUGCGGC GGCGUUAUUC CCAUGACC C GCCGGGCAGC UUCCGGGAAA CCAAAGUCUU UGGGUUCCGG GGGGAGUAUG GUUGCAAAGC UGAAACUUAA AGGAAUUGA CGGAAGGGCA CCAC(JMH)AGGAG UGGAGCCUGC GGCUUAAU(PSU)U GACUCAACAC GGGAAACCUC ACCCGGCCCG GA CACGGAC AGGAUUGACA GAUUGAUAGC UCUUUCUCGA UUCCGUGGGU GGUGGUGCAU GGCCGUUCUU AGUUGGUGGA GCG AUUUGU CUGGUUAAUU C(5MC)GAUAACGA ACGAGACUCU GGCAUGCUAA CUAGUUACGC GACCCCCGAG CGGUCGGCGU CCCCCAACU UCUUAGAGGG ACAAGUGGCG UUCAGCCACC CGAGAUUGAG CAAUAACAGG UCUGUGAUGC CCUUAGAUGU C CGGGGCUG CACGCGCGCU ACACUGACUG GCUCAGCGUG UGCCUACCCU ACGCCGGCAG GCGCGGGUAA CCCGUUGAAC CC CAUUCGU GAUGGGGAUC GGGGAUUGCA AUUAUUCCCC AUGAACGAGG AAUUCCCAGU AAGUGCGGGU CAUAAGCUUG CGU UGAUU(A2M) AGUCCCUGCC CUUUGUACAC ACCG(OMC)CCGUC GCUACUACCG AUUGGAUGGU UUAGUGAGGC CCUCGG AUC GGCCCCGCCG GGGUCGGCCC ACGGCCCUGG CGGAGCGCUG AGAAGACGGU CGAACUUGAC UAUCUAGAGG AAGUAAA AG UCG(UR3)A(6MZ)CAAG GUUUCCGUAG GUG(MA6)(MA6)CCUGC GGAAGGAUCA UUA

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Macromolecule #19: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 19 / Number of copies: 29 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #20: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 20 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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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: 7.4
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Average exposure time: 1.0 sec. / Average electron dose: 107.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
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:

4kzy

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 144882
Initial angle assignmentType: OTHER
Final angle assignmentType: OTHER
FSC plot (resolution estimation)

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