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Yorodumi- EMDB-33521: Cryo-EM structure of Fft3-nucleosome complex with Fft3 bound to S... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-33521 | |||||||||
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Title | Cryo-EM structure of Fft3-nucleosome complex with Fft3 bound to SHL+3 position of the nucleosome | |||||||||
Map data | ||||||||||
Sample |
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Keywords | DNA binding / remodeler / nucleosome / Fft3-nucleosome complex / DNA BINDING PROTEIN | |||||||||
Function / homology | Function and homology information attachment of telomeric heterochromatin to nuclear envelope / ATP-dependent H3-H4 histone complex chaperone activity / HDMs demethylate histones / Interleukin-7 signaling / PKMTs methylate histone lysines / Chromatin modifying enzymes / Condensation of Prophase Chromosomes / SUMOylation of chromatin organization proteins / RCAF complex / Metalloprotease DUBs ...attachment of telomeric heterochromatin to nuclear envelope / ATP-dependent H3-H4 histone complex chaperone activity / HDMs demethylate histones / Interleukin-7 signaling / PKMTs methylate histone lysines / Chromatin modifying enzymes / Condensation of Prophase Chromosomes / SUMOylation of chromatin organization proteins / RCAF complex / Metalloprotease DUBs / Factors involved in megakaryocyte development and platelet production / E3 ubiquitin ligases ubiquitinate target proteins / RMTs methylate histone arginines / SIRT1 negatively regulates rRNA expression / NoRC negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / RNA Polymerase I Promoter Escape / polytene chromosome band / Formation of the beta-catenin:TCF transactivating complex / PRC2 methylates histones and DNA / HDACs deacetylate histones / Transcriptional regulation by small RNAs / HATs acetylate histones / Ub-specific processing proteases / Estrogen-dependent gene expression / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / larval somatic muscle development / Senescence-Associated Secretory Phenotype (SASP) / Oxidative Stress Induced Senescence / Assembly of the ORC complex at the origin of replication / UCH proteinases / histone chaperone activity / polytene chromosome / transcription elongation-coupled chromatin remodeling / nuclear chromosome / replication fork processing / heterochromatin organization / nucleosomal DNA binding / ATP-dependent activity, acting on DNA / heterochromatin / helicase activity / structural constituent of chromatin / nucleosome / nucleosome assembly / chromosome / chromatin organization / DNA helicase / nucleic acid binding / damaged DNA binding / chromatin remodeling / protein heterodimerization activity / chromatin binding / chromatin / protein-containing complex binding / ATP hydrolysis activity / DNA binding / ATP binding / nucleus Similarity search - Function | |||||||||
Biological species | Schizosaccharomyces pombe 972h- (yeast) / Drosophila melanogaster (fruit fly) / synthetic construct (others) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.2 Å | |||||||||
Authors | Nan Z / Tao J / Yangao H | |||||||||
Funding support | China, 1 items
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Citation | Journal: To Be Published Title: Cryo-EM structure of Fft3-nucleosome complex with Fft3 bound to SHL+3 position of the nucleosome (Class II Fft3-nucleosome complex) Authors: Nan Z / Tao J / Yangao H | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_33521.map.gz | 40 MB | EMDB map data format | |
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Header (meta data) | emd-33521-v30.xml emd-33521.xml | 20.9 KB 20.9 KB | Display Display | EMDB header |
Images | emd_33521.png | 196.3 KB | ||
Filedesc metadata | emd-33521.cif.gz | 7.1 KB | ||
Others | emd_33521_half_map_1.map.gz emd_33521_half_map_2.map.gz | 33 MB 33.1 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-33521 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-33521 | HTTPS FTP |
-Related structure data
Related structure data | 7xygMC 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_33521.map.gz / Format: CCP4 / Size: 42.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.04 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_33521_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_33521_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Complex of Fft3-nucleosome complex with Fft3 bound to SHL+3 of th...
Entire | Name: Complex of Fft3-nucleosome complex with Fft3 bound to SHL+3 of the nucleosome (Class II Fft3-nucleosome complex) |
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Components |
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-Supramolecule #1: Complex of Fft3-nucleosome complex with Fft3 bound to SHL+3 of th...
Supramolecule | Name: Complex of Fft3-nucleosome complex with Fft3 bound to SHL+3 of the nucleosome (Class II Fft3-nucleosome complex) type: complex / ID: 1 / Parent: 0 / Macromolecule list: #6-#7, #1-#5 |
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Source (natural) | Organism: Schizosaccharomyces pombe 972h- (yeast) |
-Macromolecule #1: Histone H2A
Macromolecule | Name: Histone H2A / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Drosophila melanogaster (fruit fly) |
Molecular weight | Theoretical: 13.257529 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: SGRGKGGKVK GKAKSRSNRA GLQFPVGRIH RLLRKGNYAE RVGAGAPVYL AAVMEYLAAE VLELAGNAAR DNKKTRIIPR HLQLAIRND EELNKLLSGV TIAQGGVLPN IQAVLLPKKT EKKA UniProtKB: Histone H2A |
-Macromolecule #2: Histone H2B
Macromolecule | Name: Histone H2B / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Drosophila melanogaster (fruit fly) |
Molecular weight | Theoretical: 13.727064 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MPPKTSGKAA KKAGKAQKNI TKTDKKKKRK RKESYAIYIY KVLKQVHPDT GISSKAMSIM NSFVNDIFER IAAEASRLAH YNKRSTITS REIQTAVRLL LPGELAKHAV SEGTKAVTKY TSSK UniProtKB: Histone H2B |
-Macromolecule #5: ATP-dependent helicase fft3
Macromolecule | Name: ATP-dependent helicase fft3 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA helicase |
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Source (natural) | Organism: Schizosaccharomyces pombe 972h- (yeast) / Strain: 972 / ATCC 24843 |
Molecular weight | Theoretical: 104.629953 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MDGKRKIEHT ADGTHYDATS NVKRKPIFPP FIADSLSEAT EKANVMGGGM NSRLQILSEM SKRVQATAPI SSLEHFKQLS DISPSFTSS ANSINQPYNY SGSLENLVPT PSAGTPSQFM DAQNPYGAVY NALSQFSETE PKMPSYMDDE EASDSLPLSL S SQSLSSQV ...String: MDGKRKIEHT ADGTHYDATS NVKRKPIFPP FIADSLSEAT EKANVMGGGM NSRLQILSEM SKRVQATAPI SSLEHFKQLS DISPSFTSS ANSINQPYNY SGSLENLVPT PSAGTPSQFM DAQNPYGAVY NALSQFSETE PKMPSYMDDE EASDSLPLSL S SQSLSSQV TNQKPAPHRL TMRERYAANN LTNGLQFTLP LSSRKTYEPE ADDDSNDDMY SDDDSNADRW ASRIDTAALK EE VLKYMNR CSTQDLADMT GCTLAEAEFM VAKRPFPDLE SALVVKQPRP VIPKGRRGRR EKTPLGPRLV GICMEIMRGY FVV DALIRQ CEQLGGKIQR GIEAWGLSNT ATSDEGETSL VNFDQMKSFG TPANSSFITT PPASFSPDIK LQDYQIIGIN WLYL LYELK LAGILADEMG LGKTCQTIAF FSLLMDKNIN GPHLVIAPAS TMENWLREFA KFCPKLKIEL YYGSQVEREE IRERI NSNK DSYNVMLTTY RLAATSKADR LFLRNQKFNV CVYDEGHYLK NRASERYRHL MSIPADFRVL LTGTPLQNNL KELISL LAF ILPHVFDYGL KSLDVIFTMK KSPESDFERA LLSEQRVSRA KMMMAPFVLR RKKSQVLDAL PKKTRIIEFC EFSEEER RR YDDFASKQSV NSLLDENVMK TNLDTNANLA KKKSTAGFVL VQLRKLADHP MLFRIHYKDD ILRQMAKAIM NEPQYKKA N ELYIFEDMQY MSDIELHNLC CKFPSINSFQ LKDEPWMDAT KVRKLKKLLT NAVENGDRVV LFSQFTQVLD ILQLVMKSL NLKFLRFDGS TQVDFRQDLI DQFYADESIN VFLLSTKAGG FGINLACANM VILYDVSFNP FDDLQAEDRA HRVGQKKEVT VYKFVVKDT IEEHIQRLAN AKIALDATLS GNAETVEAED DDD UniProtKB: ATP-dependent helicase fft3 |
-Macromolecule #6: Histone H3
Macromolecule | Name: Histone H3 / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Drosophila melanogaster (fruit fly) |
Molecular weight | Theoretical: 15.289904 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: ARTKQTARKS TGGKAPRKQL ATKAARKSAP ATGGVKKPHR YRPGTVALRE IRRYQKSTEL LIRKLPFQRL VREIAQDFKT DLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA UniProtKB: Histone H3 |
-Macromolecule #7: Histone H4
Macromolecule | Name: Histone H4 / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Drosophila melanogaster (fruit fly) |
Molecular weight | Theoretical: 11.408452 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MTGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVY ALKRQGRTLY GFGG UniProtKB: Histone H4 |
-Macromolecule #3: DNA (167-MER)
Macromolecule | Name: DNA (167-MER) / type: dna / ID: 3 / Number of copies: 1 / Classification: DNA |
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Source (natural) | Organism: synthetic construct (others) |
Molecular weight | Theoretical: 51.783977 KDa |
Sequence | String: (DA)(DT)(DC)(DT)(DA)(DC)(DA)(DT)(DG)(DC) (DA)(DC)(DA)(DG)(DG)(DA)(DT)(DG)(DT)(DA) (DT)(DA)(DT)(DA)(DT)(DC)(DT)(DG)(DA) (DC)(DA)(DC)(DG)(DT)(DG)(DC)(DC)(DT)(DG) (DG) (DA)(DG)(DA)(DC)(DT)(DA) ...String: (DA)(DT)(DC)(DT)(DA)(DC)(DA)(DT)(DG)(DC) (DA)(DC)(DA)(DG)(DG)(DA)(DT)(DG)(DT)(DA) (DT)(DA)(DT)(DA)(DT)(DC)(DT)(DG)(DA) (DC)(DA)(DC)(DG)(DT)(DG)(DC)(DC)(DT)(DG) (DG) (DA)(DG)(DA)(DC)(DT)(DA)(DG)(DG) (DG)(DA)(DG)(DT)(DA)(DA)(DT)(DC)(DC)(DC) (DC)(DT) (DT)(DG)(DG)(DC)(DG)(DG)(DT) (DT)(DA)(DA)(DA)(DA)(DC)(DG)(DC)(DG)(DG) (DG)(DG)(DG) (DA)(DC)(DA)(DG)(DC)(DG) (DC)(DG)(DT)(DA)(DC)(DG)(DT)(DG)(DC)(DG) (DT)(DT)(DT)(DA) (DA)(DG)(DC)(DG)(DG) (DT)(DG)(DC)(DT)(DA)(DG)(DA)(DG)(DC)(DT) (DG)(DT)(DC)(DT)(DA) (DC)(DG)(DA)(DC) (DC)(DA)(DA)(DT)(DT)(DG)(DA)(DG)(DC)(DG) (DG)(DC)(DC)(DT)(DC)(DG) (DG)(DC)(DA) (DC)(DC)(DG)(DG)(DG)(DA)(DT)(DT)(DC)(DT) (DC)(DC)(DA)(DG)(DG)(DG)(DC) (DG)(DG) (DC)(DC)(DG)(DA)(DT) |
-Macromolecule #4: DNA (167-MER)
Macromolecule | Name: DNA (167-MER) / type: dna / ID: 4 / Number of copies: 1 / Classification: DNA |
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Source (natural) | Organism: synthetic construct (others) |
Molecular weight | Theoretical: 51.325676 KDa |
Sequence | String: (DA)(DT)(DC)(DG)(DG)(DC)(DC)(DG)(DC)(DC) (DC)(DT)(DG)(DG)(DA)(DG)(DA)(DA)(DT)(DC) (DC)(DC)(DG)(DG)(DT)(DG)(DC)(DC)(DG) (DA)(DG)(DG)(DC)(DC)(DG)(DC)(DT)(DC)(DA) (DA) (DT)(DT)(DG)(DG)(DT)(DC) ...String: (DA)(DT)(DC)(DG)(DG)(DC)(DC)(DG)(DC)(DC) (DC)(DT)(DG)(DG)(DA)(DG)(DA)(DA)(DT)(DC) (DC)(DC)(DG)(DG)(DT)(DG)(DC)(DC)(DG) (DA)(DG)(DG)(DC)(DC)(DG)(DC)(DT)(DC)(DA) (DA) (DT)(DT)(DG)(DG)(DT)(DC)(DG)(DT) (DA)(DG)(DA)(DC)(DA)(DG)(DC)(DT)(DC)(DT) (DA)(DG) (DC)(DA)(DC)(DC)(DG)(DC)(DT) (DT)(DA)(DA)(DA)(DC)(DG)(DC)(DA)(DC)(DG) (DT)(DA)(DC) (DG)(DC)(DG)(DC)(DT)(DG) (DT)(DC)(DC)(DC)(DC)(DC)(DG)(DC)(DG)(DT) (DT)(DT)(DT)(DA) (DA)(DC)(DC)(DG)(DC) (DC)(DA)(DA)(DG)(DG)(DG)(DG)(DA)(DT)(DT) (DA)(DC)(DT)(DC)(DC) (DC)(DT)(DA)(DG) (DT)(DC)(DT)(DC)(DC)(DA)(DG)(DG)(DC)(DA) (DC)(DG)(DT)(DG)(DT)(DC) (DA)(DG)(DA) (DT)(DA)(DT)(DA)(DT)(DA)(DC)(DA)(DT)(DC) (DC)(DT)(DG)(DT)(DG)(DC)(DA) (DT)(DG) (DT)(DA)(DG)(DA)(DT) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 1.5 µm |
Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 60.0 e/Å2 |
-Image processing
Startup model | Type of model: PDB ENTRY PDB model - PDB ID: |
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Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 49996 |