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Open data
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Basic information
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Title | Structure of the human CCAN CENP-A alpha-satellite complex | ||||||||||||
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Function / homology | ![]() spindle attachment to meiosis I kinetochore / centromeric DNA binding / CENP-A containing chromatin assembly / protein localization to chromosome, centromeric region / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | ![]() ![]() | ||||||||||||
![]() | Yatskevich S / Muir KW / Bellini D / Zhang Z / Yang J / Tischer T / Predin M / Dendooven T / McLaughlin SH / Barford D | ||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: 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. | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 91.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.1 KB 17.1 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 12.5 KB | Display | ![]() |
Images | ![]() | 56.4 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7r5rMC ![]() 7pb4C ![]() 7pb8C ![]() 7piiC ![]() 7pknC ![]() 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 ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.853 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : Human CCAN complex with bound alpha-satellite DNA
Entire | Name: Human CCAN complex with bound alpha-satellite DNA |
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Components |
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-Supramolecule #1: Human CCAN complex with bound alpha-satellite DNA
Supramolecule | Name: Human CCAN complex with bound alpha-satellite DNA / type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: #1-#7 |
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-Macromolecule #1: Histone H3-like centromeric protein A
Macromolecule | Name: Histone H3-like centromeric protein A / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 16.02363 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MGPRRRSRKP EAPRRRSPSP TPTPGPSRRG PSLGASSHQH SRRRQGWLKE IRKLQKSTHL LIRKLPFSRL AREICVKFTR GVDFNWQAQ ALLALQEAAE AFLVHLFEDA YLLTLHAGRV TLFPKDVQLA RRIRGLEEGL G |
-Macromolecule #2: Histone H4
Macromolecule | Name: Histone H4 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 11.394426 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVY ALKRQGRTLY GFGG |
-Macromolecule #3: Histone H2A type 1-C
Macromolecule | Name: Histone H2A type 1-C / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 14.135523 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIR NDEELNKLLG RVTIAQGGVL PNIQAVLLPK KTESHHKAKG K |
-Macromolecule #4: Histone H2B type 1-C/E/F/G/I
Macromolecule | Name: Histone H2B type 1-C/E/F/G/I / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 13.937213 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRST ITSREIQTAV RLLLPGELAK HAVSEGTKAV TKYTSSK |
-Macromolecule #7: Centromere protein C
Macromolecule | Name: Centromere protein C / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 61.724816 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: AASGLDHLKN GYRRRFCRPS RARDINTEQG QNVLEILQDC FEEKSLANDF STNSTKSVPN STRKIKDTCI QSPSKECQKS HPKSVPVSS KKKEASLQFV VEPSEATNRS VQAHEVHQKI LATDVSSKNT PDSKKISSRN INDHHSEADE EFYLSVGSPS V LLDAKTSV ...String: AASGLDHLKN GYRRRFCRPS RARDINTEQG QNVLEILQDC FEEKSLANDF STNSTKSVPN STRKIKDTCI QSPSKECQKS HPKSVPVSS KKKEASLQFV VEPSEATNRS VQAHEVHQKI LATDVSSKNT PDSKKISSRN INDHHSEADE EFYLSVGSPS V LLDAKTSV SQNVIPSSAQ KRETYTFENS VNMLPSSTEV SVKTKKRLNF DDKVMLKKIE IDNKVSDEED KTSEGQERKP SG SSQNRIR DSEYEIQRQA KKSFSTLFLE TVKRKSESSP IVRHAATAPP HSCPPDDTKL IEDEFIIDES DQSFASRSWI TIP RKAGSL KQRTISPAES TALLQGRKSR EKHHNILPKT LANDKHSHKP HPVETSQPSD KTVLDTSYAL IGETVNNYRS TKYE MYSKN AEKPSRSKRT IKQKQRRKFM AKPAEEQLDV GQSKDENIHT SHITQDEFQR NSDRNMEEHE EMGNDCVSKK QMPPV GSKK SSTRKDKEES KKKRFSSESK NKLVPEEVTS TVTKSRRISR RPSDWWVVKS EESPVYSNS |
-Macromolecule #5: DNA (171-MER)
Macromolecule | Name: DNA (171-MER) / type: dna / ID: 5 / Number of copies: 1 / Classification: DNA |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 52.725812 KDa |
Sequence | String: (DT)(DC)(DC)(DA)(DA)(DA)(DT)(DG)(DT)(DC) (DC)(DA)(DA)(DT)(DT)(DC)(DC)(DA)(DG)(DA) (DT)(DA)(DC)(DT)(DA)(DC)(DA)(DA)(DA) (DA)(DA)(DG)(DA)(DG)(DT)(DG)(DT)(DT)(DT) (DC) (DA)(DA)(DA)(DA)(DC)(DT) ...String: (DT)(DC)(DC)(DA)(DA)(DA)(DT)(DG)(DT)(DC) (DC)(DA)(DA)(DT)(DT)(DC)(DC)(DA)(DG)(DA) (DT)(DA)(DC)(DT)(DA)(DC)(DA)(DA)(DA) (DA)(DA)(DG)(DA)(DG)(DT)(DG)(DT)(DT)(DT) (DC) (DA)(DA)(DA)(DA)(DC)(DT)(DG)(DC) (DT)(DC)(DT)(DA)(DT)(DG)(DA)(DA)(DA)(DA) (DG)(DG) (DA)(DA)(DT)(DG)(DT)(DT)(DC) (DA)(DA)(DC)(DT)(DC)(DT)(DA)(DT)(DG)(DA) (DG)(DT)(DT) (DG)(DA)(DA)(DT)(DG)(DC) (DA)(DA)(DA)(DC)(DA)(DT)(DC)(DA)(DC)(DA) (DT)(DA)(DG)(DA) (DA)(DG)(DT)(DT)(DT) (DC)(DT)(DG)(DA)(DG)(DA)(DA)(DT)(DG)(DC) (DT)(DT)(DC)(DT)(DG) (DT)(DC)(DT)(DA) (DG)(DT)(DT)(DT)(DT)(DT)(DA)(DT)(DG)(DT) (DG)(DA)(DA)(DC)(DA)(DT) (DA)(DT)(DT) (DC)(DC)(DC)(DG)(DT)(DT)(DT)(DC)(DC)(DA) (DA)(DC)(DG)(DA)(DA)(DG)(DG) (DC)(DC) (DT)(DC)(DA)(DA)(DA)(DG)(DC)(DG)(DG) |
-Macromolecule #6: DNA (171-MER)
Macromolecule | Name: DNA (171-MER) / type: dna / ID: 6 / Number of copies: 1 / Classification: DNA |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 52.822809 KDa |
Sequence | String: (DC)(DC)(DG)(DC)(DT)(DT)(DT)(DG)(DA)(DG) (DG)(DC)(DC)(DT)(DT)(DC)(DG)(DT)(DT)(DG) (DG)(DA)(DA)(DA)(DC)(DG)(DG)(DG)(DA) (DA)(DT)(DA)(DT)(DG)(DT)(DT)(DC)(DA)(DC) (DA) (DT)(DA)(DA)(DA)(DA)(DA) ...String: (DC)(DC)(DG)(DC)(DT)(DT)(DT)(DG)(DA)(DG) (DG)(DC)(DC)(DT)(DT)(DC)(DG)(DT)(DT)(DG) (DG)(DA)(DA)(DA)(DC)(DG)(DG)(DG)(DA) (DA)(DT)(DA)(DT)(DG)(DT)(DT)(DC)(DA)(DC) (DA) (DT)(DA)(DA)(DA)(DA)(DA)(DC)(DT) (DA)(DG)(DA)(DC)(DA)(DG)(DA)(DA)(DG)(DC) (DA)(DT) (DT)(DC)(DT)(DC)(DA)(DG)(DA) (DA)(DA)(DC)(DT)(DT)(DC)(DT)(DA)(DT)(DG) (DT)(DG)(DA) (DT)(DG)(DT)(DT)(DT)(DG) (DC)(DA)(DT)(DT)(DC)(DA)(DA)(DC)(DT)(DC) (DA)(DT)(DA)(DG) (DA)(DG)(DT)(DT)(DG) (DA)(DA)(DC)(DA)(DT)(DT)(DC)(DC)(DT)(DT) (DT)(DT)(DC)(DA)(DT) (DA)(DG)(DA)(DG) (DC)(DA)(DG)(DT)(DT)(DT)(DT)(DG)(DA)(DA) (DA)(DC)(DA)(DC)(DT)(DC) (DT)(DT)(DT) (DT)(DT)(DG)(DT)(DA)(DG)(DT)(DA)(DT)(DC) (DT)(DG)(DG)(DA)(DA)(DT)(DT) (DG)(DG) (DA)(DC)(DA)(DT)(DT)(DT)(DG)(DG)(DA) |
-Experimental details
-Structure determination
Method | ![]() |
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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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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 40.0 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |