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Open data
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Basic information
| Entry | ![]() | ||||||||||||
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| Title | Structure of the human CCAN deltaCT complex | ||||||||||||
Map data | 3D consensus refinement | ||||||||||||
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Keywords | Kinetochore / chromosome segregation / centromere / CELL CYCLE | ||||||||||||
| Function / homology | Function and homology informationMis6-Sim4 complex / positive regulation of protein localization to kinetochore / : / kinetochore organization / metaphase chromosome alignment / kinetochore binding / CENP-A containing chromatin assembly / sex differentiation / chordate embryonic development / negative regulation of epithelial cell apoptotic process ...Mis6-Sim4 complex / positive regulation of protein localization to kinetochore / : / kinetochore organization / metaphase chromosome alignment / kinetochore binding / CENP-A containing chromatin assembly / sex differentiation / chordate embryonic development / negative regulation of epithelial cell apoptotic process / kinetochore assembly / inner kinetochore / mitotic sister chromatid segregation / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Deposition of new CENPA-containing nucleosomes at the centromere / NRIF signals cell death from the nucleus / Resolution of Sister Chromatid Cohesion / positive regulation of epithelial cell proliferation / mitotic spindle organization / chromosome segregation / RHO GTPases Activate Formins / kinetochore / centriolar satellite / Separation of Sister Chromatids / actin cytoskeleton / chromosome / cell adhesion / nuclear body / cell division / apoptotic process / regulation of DNA-templated transcription / nucleolus / signal transduction / nucleoplasm / nucleus / membrane / cytoplasm / cytosol Similarity search - Function | ||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.2 Å | ||||||||||||
Authors | Muir KW / Yatskevich S / Bellini D / Barford D | ||||||||||||
| Funding support | Germany, 3 items
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Citation | Journal: Science / Year: 2022Title: Structure of the human inner kinetochore bound to a centromeric CENP-A nucleosome. Authors: Stanislau Yatskevich / Kyle W Muir / Dom Bellini / Ziguo Zhang / Jing Yang / Thomas Tischer / Masa Predin / Tom Dendooven / Stephen H McLaughlin / David Barford / ![]() Abstract: Kinetochores assemble onto specialized centromeric CENP-A (centromere protein A) nucleosomes (CENP-A) to mediate attachments between chromosomes and the mitotic spindle. We describe cryo-electron ...Kinetochores assemble onto specialized centromeric CENP-A (centromere protein A) nucleosomes (CENP-A) to mediate attachments between chromosomes and the mitotic spindle. We describe cryo-electron microscopy structures of the human inner kinetochore constitutive centromere associated network (CCAN) complex bound to CENP-A reconstituted onto α-satellite DNA. CCAN forms edge-on contacts with CENP-A, and a linker DNA segment of the α-satellite repeat emerges from the fully wrapped end of the nucleosome to thread through the central CENP-LN channel that tightly grips the DNA. The CENP-TWSX histone-fold module further augments DNA binding and partially wraps the linker DNA in a manner reminiscent of canonical nucleosomes. Our study suggests that the topological entrapment of the linker DNA by CCAN provides a robust mechanism by which kinetochores withstand both pushing and pulling forces exerted by the mitotic spindle. | ||||||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_13473.map.gz | 15.1 MB | EMDB map data format | |
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| Header (meta data) | emd-13473-v30.xml emd-13473.xml | 31.8 KB 31.8 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_13473_fsc.xml | 12.1 KB | Display | FSC data file |
| Images | emd_13473.png | 52.5 KB | ||
| Filedesc metadata | emd-13473.cif.gz | 8.2 KB | ||
| Others | emd_13473_additional_1.map.gz emd_13473_additional_2.map.gz emd_13473_additional_3.map.gz emd_13473_additional_4.map.gz | 9.9 MB 9.4 MB 10.8 MB 116.6 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-13473 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-13473 | HTTPS FTP |
-Validation report
| Summary document | emd_13473_validation.pdf.gz | 399.8 KB | Display | EMDB validaton report |
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| Full document | emd_13473_full_validation.pdf.gz | 399.3 KB | Display | |
| Data in XML | emd_13473_validation.xml.gz | 12.7 KB | Display | |
| Data in CIF | emd_13473_validation.cif.gz | 17 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-13473 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-13473 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7pknMC ![]() 7pb4C ![]() 7pb8C ![]() 7piiC ![]() 7r5rC ![]() 7r5sC ![]() 7r5vC ![]() 7ywxC ![]() 7yyhC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_13473.map.gz / Format: CCP4 / Size: 149.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | 3D consensus refinement | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.86 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: HIKMLN body
| File | emd_13473_additional_1.map | ||||||||||||
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| Annotation | HIKMLN body | ||||||||||||
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-Additional map: OPQURN body
| File | emd_13473_additional_2.map | ||||||||||||
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| Annotation | OPQURN body | ||||||||||||
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-Additional map: OPQURN focused refinement
| File | emd_13473_additional_3.map | ||||||||||||
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| Annotation | OPQURN focused refinement | ||||||||||||
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-Additional map: Combined focused map from PHENIX
| File | emd_13473_additional_4.map | ||||||||||||
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| Annotation | Combined focused map from PHENIX | ||||||||||||
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Sample components
+Entire : Human inner kinetochore CCAN
+Supramolecule #1: Human inner kinetochore CCAN
+Macromolecule #1: Centromere protein H
+Macromolecule #2: Centromere protein I
+Macromolecule #3: Centromere protein K
+Macromolecule #4: Centromere protein L
+Macromolecule #5: Centromere protein M
+Macromolecule #6: Centromere protein N
+Macromolecule #7: Centromere protein O
+Macromolecule #8: Centromere protein P
+Macromolecule #9: Centromere protein Q
+Macromolecule #10: Centromere protein U
+Macromolecule #11: Centromere protein R
+Macromolecule #12: water
-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: 7.8 |
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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: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Homo sapiens (human)
Authors
Germany, 3 items
Citation






















Z (Sec.)
Y (Row.)
X (Col.)




















































Trichoplusia ni (cabbage looper)
Processing
FIELD EMISSION GUN

