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Open data
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Basic information
| Entry | Database: PDB / ID: 8ifg | ||||||||||||||||||||||||
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| Title | Cryo-EM structure of the Clr6S (Clr6-HDAC) complex from S. pombe | ||||||||||||||||||||||||
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Keywords | TRANSCRIPTION / Rpd3S / Histone deacetylase / HDAC / Clr6 / Rpd3 / Clr6S / Clr6 HDAC | ||||||||||||||||||||||||
| Function / homology | Function and homology informationhistone H4K16 deacetylase activity, hydrolytic mechanism / histone H4K5 deacetylase activity, hydrolytic mechanism / histone H4K8 deacetylase activity, hydrolytic mechanism / histone H3K14 deacetylase activity, hydrolytic mechanism / HDACs deacetylate histones / histone H4K12 deacetylase activity, hydrolytic mechanism / SUMOylation of chromatin organization proteins / H3-H4 histone complex chaperone activity / histone H3K9 deacetylase activity, hydrolytic mechanism / Rpd3L complex ...histone H4K16 deacetylase activity, hydrolytic mechanism / histone H4K5 deacetylase activity, hydrolytic mechanism / histone H4K8 deacetylase activity, hydrolytic mechanism / histone H3K14 deacetylase activity, hydrolytic mechanism / HDACs deacetylate histones / histone H4K12 deacetylase activity, hydrolytic mechanism / SUMOylation of chromatin organization proteins / H3-H4 histone complex chaperone activity / histone H3K9 deacetylase activity, hydrolytic mechanism / Rpd3L complex / Rpd3L-Expanded complex / Rpd3S complex / histone deacetylase / protein lysine deacetylase activity / histone deacetylase activity / DNA repair-dependent chromatin remodeling / Sin3-type complex / NuA4 histone acetyltransferase complex / transcription initiation-coupled chromatin remodeling / epigenetic regulation of gene expression / mitotic spindle / transcription corepressor activity / heterochromatin formation / histone binding / molecular adaptor activity / chromatin remodeling / DNA repair / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / chromatin / negative regulation of transcription by RNA polymerase II / zinc ion binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | ||||||||||||||||||||||||
Authors | Zhang, H.Q. / Wang, X. / Wang, Y.N. / Liu, S.M. / Zhang, Y. / Xu, K. / Ji, L.T. / Kornberg, R.D. | ||||||||||||||||||||||||
| Funding support | 1items
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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
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8ifg.cif.gz | 454.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8ifg.ent.gz | 351 KB | Display | PDB format |
| PDBx/mmJSON format | 8ifg.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/if/8ifg ftp://data.pdbj.org/pub/pdb/validation_reports/if/8ifg | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 35416MC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-Protein , 6 types, 7 molecules BACEDFP
| #1: Protein | Mass: 48528.926 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: prw1, SPAC29A4.18 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: O14021 | ||||
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| #2: Protein | Mass: 125011.609 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: pst2, SPAC23C11.15 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: O13919 | ||||
| #3: Protein | Mass: 45773.371 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: clr6, SPBC36.05c / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: O59702, histone deacetylase | ||||
| #4: Protein | Mass: 39191.199 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: alp13, eaf3, SPAC23H4.12 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: O13953#5: Protein | | Mass: 45046.082 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: SPAC16C9.05 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q09819#6: Protein | | Mass: 68871.703 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: SPAC2F7.07c / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q09698 |
-Non-polymers , 2 types, 4 molecules 


| #7: Chemical | | #8: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Cryo-EM structure of the Clr6-HDAC (Clr6S) complex from S. pombe Type: COMPLEX / Entity ID: #1-#6 / Source: RECOMBINANT |
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| Molecular weight | Value: 0.6 MDa / Experimental value: YES |
| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: Trichoplusia ni (cabbage looper) |
| Buffer solution | pH: 8 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 721645 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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PDBj
Trichoplusia ni (cabbage looper)
FIELD EMISSION GUN