+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-17251 | ||||||||||||
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Title | Structure of apo telomeric nucleosome | ||||||||||||
Map data | Postprocess map of Apo-TeloNCP | ||||||||||||
Sample |
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Keywords | Telomeric nucleosome / shelterin / telomere / DNA BINDING PROTEIN | ||||||||||||
Function / homology | Function and homology information negative regulation of megakaryocyte differentiation / protein localization to CENP-A containing chromatin / Chromatin modifying enzymes / Replacement of protamines by nucleosomes in the male pronucleus / CENP-A containing nucleosome / epigenetic regulation of gene expression / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Deposition of new CENPA-containing nucleosomes at the centromere ...negative regulation of megakaryocyte differentiation / protein localization to CENP-A containing chromatin / Chromatin modifying enzymes / Replacement of protamines by nucleosomes in the male pronucleus / CENP-A containing nucleosome / epigenetic regulation of gene expression / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Deposition of new CENPA-containing nucleosomes at the centromere / nucleosomal DNA binding / heterochromatin formation / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / Inhibition of DNA recombination at telomere / Meiotic synapsis / telomere organization / RNA Polymerase I Promoter Opening / Interleukin-7 signaling / Assembly of the ORC complex at the origin of replication / SUMOylation of chromatin organization proteins / DNA methylation / Condensation of Prophase Chromosomes / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / SIRT1 negatively regulates rRNA expression / Chromatin modifications during the maternal to zygotic transition (MZT) / HCMV Late Events / innate immune response in mucosa / PRC2 methylates histones and DNA / Defective pyroptosis / HDACs deacetylate histones / RNA Polymerase I Promoter Escape / Nonhomologous End-Joining (NHEJ) / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / NoRC negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / B-WICH complex positively regulates rRNA expression / G2/M DNA damage checkpoint / HDMs demethylate histones / DNA Damage/Telomere Stress Induced Senescence / Metalloprotease DUBs / PKMTs methylate histone lysines / Meiotic recombination / RMTs methylate histone arginines / Pre-NOTCH Transcription and Translation / Activation of anterior HOX genes in hindbrain development during early embryogenesis / HCMV Early Events / Transcriptional regulation of granulopoiesis / structural constituent of chromatin / antimicrobial humoral immune response mediated by antimicrobial peptide / UCH proteinases / nucleosome / nucleosome assembly / E3 ubiquitin ligases ubiquitinate target proteins / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / chromatin organization / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Factors involved in megakaryocyte development and platelet production / gene expression / HATs acetylate histones / Processing of DNA double-strand break ends / antibacterial humoral response / Senescence-Associated Secretory Phenotype (SASP) / Oxidative Stress Induced Senescence / Estrogen-dependent gene expression / chromosome, telomeric region / Ub-specific processing proteases / defense response to Gram-positive bacterium / cadherin binding / protein heterodimerization activity / Amyloid fiber formation / negative regulation of cell population proliferation / protein-containing complex / DNA binding / RNA binding / extracellular space / extracellular exosome / extracellular region / nucleoplasm / identical protein binding / membrane / nucleus / cytosol Similarity search - Function | ||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.52 Å | ||||||||||||
Authors | Hu H / van Roon AMM / Ghanim GE / Ahsan B / Oluwole A / Peak-Chew S / Robinson CV / Nguyen THD | ||||||||||||
Funding support | United Kingdom, European Union, United States, 3 items
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Citation | Journal: Sci Adv / Year: 2023 Title: Structural basis of telomeric nucleosome recognition by shelterin factor TRF1. Authors: Hongmiao Hu / Anne-Marie M van Roon / George E Ghanim / Bilal Ahsan / Abraham O Oluwole / Sew-Yeu Peak-Chew / Carol V Robinson / Thi Hoang Duong Nguyen / Abstract: Shelterin and nucleosomes are the key players that organize mammalian chromosome ends into the protective telomere caps. However, how they interact with each other at telomeres remains unknown. We ...Shelterin and nucleosomes are the key players that organize mammalian chromosome ends into the protective telomere caps. However, how they interact with each other at telomeres remains unknown. We report cryo-electron microscopy structures of a human telomeric nucleosome both unbound and bound to the shelterin factor TRF1. Our structures reveal that TRF1 binds unwrapped nucleosomal DNA ends by engaging both the nucleosomal DNA and the histone octamer. Unexpectedly, TRF1 binding shifts the register of the nucleosomal DNA by 1 bp. We discovered that phosphorylation of the TRF1 C terminus and a noncanomical DNA binding surface on TRF1 are critical for its association with telomeric nucleosomes. These insights into shelterin-chromatin interactions have crucial implications for understanding telomeric chromatin organization and other roles of shelterin at telomeres including replication and transcription. | ||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_17251.map.gz | 93.6 MB | EMDB map data format | |
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Header (meta data) | emd-17251-v30.xml emd-17251.xml | 28.2 KB 28.2 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_17251_fsc.xml | 10.7 KB | Display | FSC data file |
Images | emd_17251.png | 83.9 KB | ||
Others | emd_17251_additional_1.map.gz emd_17251_half_map_1.map.gz emd_17251_half_map_2.map.gz | 81 MB 81.2 MB 81.2 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-17251 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-17251 | HTTPS FTP |
-Validation report
Summary document | emd_17251_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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Full document | emd_17251_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | emd_17251_validation.xml.gz | 17.6 KB | Display | |
Data in CIF | emd_17251_validation.cif.gz | 23.2 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17251 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17251 | HTTPS FTP |
-Related structure data
Related structure data | 8ox0MC 8ox1C M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_17251.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Annotation | Postprocess map of Apo-TeloNCP | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.73 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: Refine3D map of Apo-TeloNCP
File | emd_17251_additional_1.map | ||||||||||||
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Annotation | Refine3D map of Apo-TeloNCP | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Refine3D half map of Apo-TeloNCP
File | emd_17251_half_map_1.map | ||||||||||||
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Annotation | Refine3D half map of Apo-TeloNCP | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Refine3D half map of Apo-TeloNCP
File | emd_17251_half_map_2.map | ||||||||||||
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Annotation | Refine3D half map of Apo-TeloNCP | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : TRF1core in complex with telomeric nucleosome
Entire | Name: TRF1core in complex with telomeric nucleosome |
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Components |
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-Supramolecule #1: TRF1core in complex with telomeric nucleosome
Supramolecule | Name: TRF1core in complex with telomeric nucleosome / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#6 |
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-Supramolecule #2: Human telomeric nucleosome
Supramolecule | Name: Human telomeric nucleosome / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#6 Details: Human telomeric nucleosome with 145 bp DNA and human histone octamer. 145 bp DNA consists of 23 copies of TTAGGG repeats. Histone octamer consists of 2 copies of H2A, H2B, H3 and H4 |
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Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Histone H3.1
Macromolecule | Name: Histone H3.1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 15.805581 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: GPRGMARTKQ TARKSTGGKA PRKQLATKAA RKSAPATGGV KKPHRYRPGT VALREIRRYQ KSTELLIRKL PFQRLVREIA QDFKTDLRF QSSAVMALQE ACEAYLVGLF EDTNLCAIHA KRVTIMPKDI QLARRIRGER A UniProtKB: Histone H3.1 |
-Macromolecule #2: Histone H4
Macromolecule | Name: Histone H4 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 11.762839 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: GPRGMSGRGK GGKGLGKGGA KRHRKVLRDN IQGITKPAIR RLARRGGVKR ISGLIYEETR GVLKVFLENV IRDAVTYTEH AKRKTVTAM DVVYALKRQG RTLYGFGG UniProtKB: Histone H4 |
-Macromolecule #3: Histone H2A type 1-C
Macromolecule | Name: Histone H2A type 1-C / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 14.503938 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: GPRGMSGRGK QGGKARAKAK SRSSRAGLQF PVGRVHRLLR KGNYAERVGA GAPVYLAAVL EYLTAEILEL AGNAARDNKK TRIIPRHLQ LAIRNDEELN KLLGRVTIAQ GGVLPNIQAV LLPKKTESHH KAKGK UniProtKB: Histone H2A type 1-C |
-Macromolecule #4: Histone H2B type 1-C/E/F/G/I
Macromolecule | Name: Histone H2B type 1-C/E/F/G/I / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 14.305627 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: GPRGMPEPAK SAPAPKKGSK KAVTKAQKKD GKKRKRSRKE SYSVYVYKVL KQVHPDTGIS SKAMGIMNSF VNDIFERIAG EASRLAHYN KRSTITSREI QTAVRLLLPG ELAKHAVSEG TKAVTKYTSS K UniProtKB: Histone H2B type 1-C/E/F/G/I |
-Macromolecule #5: Telomeric DNA G strand
Macromolecule | Name: Telomeric DNA G strand / type: dna / ID: 5 / Number of copies: 1 / Classification: DNA |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 46.024258 KDa |
Sequence | String: (DA)(DT)(DC)(DT)(DT)(DA)(DG)(DG)(DG)(DT) (DT)(DA)(DG)(DG)(DG)(DT)(DT)(DA)(DG)(DG) (DG)(DT)(DT)(DA)(DG)(DG)(DG)(DT)(DT) (DA)(DG)(DG)(DG)(DT)(DT)(DA)(DG)(DG)(DG) (DT) (DT)(DA)(DG)(DG)(DG)(DT) ...String: (DA)(DT)(DC)(DT)(DT)(DA)(DG)(DG)(DG)(DT) (DT)(DA)(DG)(DG)(DG)(DT)(DT)(DA)(DG)(DG) (DG)(DT)(DT)(DA)(DG)(DG)(DG)(DT)(DT) (DA)(DG)(DG)(DG)(DT)(DT)(DA)(DG)(DG)(DG) (DT) (DT)(DA)(DG)(DG)(DG)(DT)(DT)(DA) (DG)(DG)(DG)(DT)(DT)(DA)(DG)(DG)(DG)(DT) (DT)(DA) (DG)(DG)(DG)(DT)(DT)(DA)(DG) (DG)(DG)(DT)(DT)(DA)(DG)(DG)(DG)(DT)(DT) (DA)(DG)(DG) (DG)(DT)(DT)(DA)(DG)(DG) (DG)(DT)(DT)(DA)(DG)(DG)(DG)(DT)(DT)(DA) (DG)(DG)(DG)(DT) (DT)(DA)(DG)(DG)(DG) (DT)(DT)(DA)(DG)(DG)(DG)(DT)(DT)(DA)(DG) (DG)(DG)(DT)(DT)(DA) (DG)(DG)(DG)(DT) (DT)(DA)(DG)(DG)(DG)(DT)(DT)(DA)(DG)(DG) (DG)(DT)(DT)(DA)(DG)(DG) (DG)(DT)(DG) (DA)(DT) |
-Macromolecule #6: Telomeric DNA C strand
Macromolecule | Name: Telomeric DNA C strand / type: dna / ID: 6 / Number of copies: 1 / Classification: DNA |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 43.478914 KDa |
Sequence | String: (DA)(DT)(DC)(DA)(DC)(DC)(DC)(DT)(DA)(DA) (DC)(DC)(DC)(DT)(DA)(DA)(DC)(DC)(DC)(DT) (DA)(DA)(DC)(DC)(DC)(DT)(DA)(DA)(DC) (DC)(DC)(DT)(DA)(DA)(DC)(DC)(DC)(DT)(DA) (DA) (DC)(DC)(DC)(DT)(DA)(DA) ...String: (DA)(DT)(DC)(DA)(DC)(DC)(DC)(DT)(DA)(DA) (DC)(DC)(DC)(DT)(DA)(DA)(DC)(DC)(DC)(DT) (DA)(DA)(DC)(DC)(DC)(DT)(DA)(DA)(DC) (DC)(DC)(DT)(DA)(DA)(DC)(DC)(DC)(DT)(DA) (DA) (DC)(DC)(DC)(DT)(DA)(DA)(DC)(DC) (DC)(DT)(DA)(DA)(DC)(DC)(DC)(DT)(DA)(DA) (DC)(DC) (DC)(DT)(DA)(DA)(DC)(DC)(DC) (DT)(DA)(DA)(DC)(DC)(DC)(DT)(DA)(DA)(DC) (DC)(DC)(DT) (DA)(DA)(DC)(DC)(DC)(DT) (DA)(DA)(DC)(DC)(DC)(DT)(DA)(DA)(DC)(DC) (DC)(DT)(DA)(DA) (DC)(DC)(DC)(DT)(DA) (DA)(DC)(DC)(DC)(DT)(DA)(DA)(DC)(DC)(DC) (DT)(DA)(DA)(DC)(DC) (DC)(DT)(DA)(DA) (DC)(DC)(DC)(DT)(DA)(DA)(DC)(DC)(DC)(DT) (DA)(DA)(DC)(DC)(DC)(DT) (DA)(DA)(DG) (DA)(DT) |
-Macromolecule #7: water
Macromolecule | Name: water / type: ligand / ID: 7 / Number of copies: 57 / Formula: HOH |
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Molecular weight | Theoretical: 18.015 Da |
Chemical component information | ChemComp-HOH: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 Component:
Details: 25 mM HEPES-KOH pH 8.0, 150 mM KCl, 1 mM MgCl2, 1% glycerol, 0.01% Igepal CA-630,1 mM DTT | |||||||||||||||||||||
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Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 70 sec. | |||||||||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV / Details: Blot Force: -15 Blot Time: 2.5 s. |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Temperature | Min: 78.0 K |
Specialist optics | Energy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 12126 / Average exposure time: 1.15 sec. / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 105000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Software | Name: UCSF ChimeraX (ver. 1.5) |
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Output model | PDB-8ox0: |