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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-25180 | |||||||||
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| Title | SMARCAD1-nucleosome map 1 | |||||||||
Map data | ||||||||||
Sample |
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| Biological species | Homo sapiens (human) / synthetic construct (others) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 6.49 Å | |||||||||
Authors | Markert J / Luger K | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Sci Adv / Year: 2021Title: SMARCAD1 is an ATP-dependent histone octamer exchange factor with de novo nucleosome assembly activity. Authors: Jonathan Markert / Keda Zhou / Karolin Luger / ![]() Abstract: The adenosine 5′-triphosphate (ATP)–dependent chromatin remodeler SMARCAD1 acts on nucleosomes during DNA replication, repair, and transcription, but despite its implication in disease, ...The adenosine 5′-triphosphate (ATP)–dependent chromatin remodeler SMARCAD1 acts on nucleosomes during DNA replication, repair, and transcription, but despite its implication in disease, information on its function and biochemical activities is scarce. Chromatin remodelers use the energy of ATP hydrolysis to slide nucleosomes, evict histones, or exchange histone variants. Here, we show that SMARCAD1 transfers the entire histone octamer from one DNA segment to another in an ATP-dependent manner but is also capable of de novo nucleosome assembly from histone octamer because of its ability to simultaneously bind all histones. We present a low-resolution cryo–electron microscopy structure of SMARCAD1 in complex with a nucleosome and show that the adenosine triphosphatase domains engage their substrate unlike any other chromatin remodeler. Our biochemical and structural data provide mechanistic insights into SMARCAD1-induced nucleosome disassembly and reassembly. | |||||||||
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Structure visualization
| Movie |
Movie viewer |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_25180.map.gz | 49.1 MB | EMDB map data format | |
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| Header (meta data) | emd-25180-v30.xml emd-25180.xml | 8.1 KB 8.1 KB | Display Display | EMDB header |
| Images | emd_25180.png | 33.9 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-25180 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-25180 | HTTPS FTP |
-Related structure data
| Related structure data | C: citing same article ( |
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| Similar structure data | |
| EM raw data | EMPIAR-10939 (Title: Cryo electron microscopy SMARCAD1 with nucleosome in ADP-BeF3 bound stateData size: 6.2 TB Data #1: Unaligned multi-frame micrographs of SMARCAD1-nucleosome with ADP-BeF3 [micrographs - multiframe]) |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_25180.map.gz / Format: CCP4 / Size: 64 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: 1.065 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : SMARCAD1-nucleosome
| Entire | Name: SMARCAD1-nucleosome |
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| Components |
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-Supramolecule #1: SMARCAD1-nucleosome
| Supramolecule | Name: SMARCAD1-nucleosome / type: complex / ID: 1 / Parent: 0 |
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-Supramolecule #2: SMARCAD1
| Supramolecule | Name: SMARCAD1 / type: complex / ID: 2 / Parent: 1 |
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| Source (natural) | Organism: Homo sapiens (human) |
| Recombinant expression | Organism: ![]() |
-Supramolecule #3: nucleosome histones
| Supramolecule | Name: nucleosome histones / type: complex / ID: 3 / Parent: 1 |
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| Source (natural) | Organism: Homo sapiens (human) |
| Recombinant expression | Organism: ![]() |
-Supramolecule #4: nucleosome DNA
| Supramolecule | Name: nucleosome DNA / type: complex / ID: 4 / Parent: 1 |
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| Source (natural) | Organism: synthetic construct (others) |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 1.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 6.49 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 20135 |
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| Initial angle assignment | Type: ANGULAR RECONSTITUTION |
| Final angle assignment | Type: ANGULAR RECONSTITUTION |
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About Yorodumi



Homo sapiens (human)
Authors
United States, 1 items
Citation
UCSF Chimera








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