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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Rpd3S-nucleosome (H3K36me3 modified) | |||||||||
Map data | Rpd3S-H3K36me3-NCP | |||||||||
Sample |
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Keywords | Rpd3S / nucleosome / HDAC / deacetylation / TRANSCRIPTION | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 4.6 Å | |||||||||
Authors | Wang X / Wang YN / Liu SM / Zhang Y / Xu K / Ji LT / Kornberg RD / Zhang HQ | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2023Title: Class I histone deacetylase complex: Structure and functional correlates. Authors: Xiao Wang / Yannan Wang / Simiao Liu / Yi Zhang / Ke Xu / Liting Ji / Roger D Kornberg / Heqiao Zhang / ![]() Abstract: The Clr6S complex, a class I histone deacetylase complex, functions as a zinc-dependent enzyme to remove acetyl groups from lysine residues in histone tails. We report here the cryo-EM structure of ...The Clr6S complex, a class I histone deacetylase complex, functions as a zinc-dependent enzyme to remove acetyl groups from lysine residues in histone tails. We report here the cryo-EM structure of Clr6S alone and a cryo-EM map of Clr6S in complex with a nucleosome. The active center, revealed at near-atomic resolution, includes features important for catalysis-A water molecule coordinated by zinc, the likely nucleophile for attack on the acetyl-lysine bond, and a loop that may position the substrate for catalysis. The cryo-EM map in the presence of a nucleosome reveals multiple Clr6S-nucleosome contacts and a high degree of relative motion of Clr6S and the nucleosome. Such flexibility may be attributed to interaction at a site in the flexible histone tail and is likely important for the function of the deacetylase, which acts at multiple sites in other histone tails. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_36278.map.gz | 51.1 MB | EMDB map data format | |
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| Header (meta data) | emd-36278-v30.xml emd-36278.xml | 12.4 KB 12.4 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_36278_fsc.xml | 11.2 KB | Display | FSC data file |
| Images | emd_36278.png | 30.9 KB | ||
| Filedesc metadata | emd-36278.cif.gz | 3.8 KB | ||
| Others | emd_36278_half_map_1.map.gz emd_36278_half_map_2.map.gz | 95.7 MB 95.7 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-36278 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-36278 | HTTPS FTP |
-Validation report
| Summary document | emd_36278_validation.pdf.gz | 1.2 MB | Display | EMDB validaton report |
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| Full document | emd_36278_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | emd_36278_validation.xml.gz | 18.4 KB | Display | |
| Data in CIF | emd_36278_validation.cif.gz | 23.6 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-36278 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-36278 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_36278.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Rpd3S-H3K36me3-NCP | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.06 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: Half map B
| File | emd_36278_half_map_1.map | ||||||||||||
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| Annotation | Half map B | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Half map A
| File | emd_36278_half_map_2.map | ||||||||||||
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| Annotation | Half map A | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Rpd3S complexed with H3K36me3 modified nucleosome
| Entire | Name: Rpd3S complexed with H3K36me3 modified nucleosome |
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| Components |
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-Supramolecule #1: Rpd3S complexed with H3K36me3 modified nucleosome
| Supramolecule | Name: Rpd3S complexed with H3K36me3 modified nucleosome / type: complex / ID: 1 / Parent: 0 |
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| Source (natural) | Organism: ![]() |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 1 mg/mL |
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| Buffer | pH: 8 |
| 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: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: OTHER / Imaging mode: OTHER / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.2 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
China, 1 items
Citation



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Y (Row.)
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Processing
FIELD EMISSION GUN

