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- EMDB-10159: Class 1C : CENP-A nucleosome -

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Basic information

Entry
Database: EMDB / ID: EMD-10159
TitleClass 1C : CENP-A nucleosome
Map data
SampleClass 1C : CENP-A nucleosome
Function / homology
Function and homology information


condensed chromosome inner kinetochore / kinetochore assembly / protein localization to chromosome, centromeric region / pericentric heterochromatin => GO:0005721 / condensed nuclear chromosome kinetochore / condensed chromosome, centromeric region => GO:0000779 / establishment of mitotic spindle orientation / negative regulation of megakaryocyte differentiation / CENP-A containing nucleosome assembly / chromosome, centromeric region ...condensed chromosome inner kinetochore / kinetochore assembly / protein localization to chromosome, centromeric region / pericentric heterochromatin => GO:0005721 / condensed nuclear chromosome kinetochore / condensed chromosome, centromeric region => GO:0000779 / establishment of mitotic spindle orientation / negative regulation of megakaryocyte differentiation / CENP-A containing nucleosome assembly / chromosome, centromeric region / DNA replication-independent nucleosome assembly / telomere capping / mitotic cytokinesis / chromatin silencing / telomere organization / DNA replication-dependent nucleosome assembly / nucleosome => GO:0000786 / innate immune response in mucosa / rDNA heterochromatin assembly / negative regulation of gene expression, epigenetic / regulation of gene silencing by miRNA / nuclear chromosome / DNA-templated transcription, initiation / regulation of megakaryocyte differentiation / nucleosome assembly / nucleosome / double-strand break repair via nonhomologous end joining / chromatin organization / chromosome, telomeric region => GO:0000781 / antibacterial humoral response / antimicrobial humoral immune response mediated by antimicrobial peptide / protein ubiquitination / protein heterodimerization activity / defense response to Gram-positive bacterium / chromatin => GO:0000785 / protein domain specific binding / chromatin binding / cellular protein metabolic process / viral process / protein-containing complex / RNA binding / DNA binding / extracellular space / extracellular exosome / membrane / extracellular region / nucleoplasm / identical protein binding / nucleus / cytosol
Histone H4 / Histone H2A / Histone H4, conserved site / Histone H2A, C-terminal domain / Histone H2A conserved site / TATA box binding protein associated factor (TAF) / CENP-T/Histone H4, histone fold / Histone H2B / Histone H2A/H2B/H3 / Histone H3/CENP-A / Histone-fold
Histone H3-like centromeric protein A / Histone H4 / Histone H2B type 1-C/E/F/G/I / Histone H2A type 2-A
Methodsingle particle reconstruction / cryo EM / Resolution: 4.2 Å
AuthorsAli-Ahmad A / Bilokapic S / Halic M / Sekulic N
Funding support Norway, Germany, 2 items
OrganizationGrant numberCountry
Norwegian Research Council263195 Norway
European Research CouncilERC-smallRNAhet-309584 Germany
CitationJournal: EMBO Rep / Year: 2019
Title: CENP-C unwraps the human CENP-A nucleosome through the H2A C-terminal tail.
Authors: Ahmad Ali-Ahmad / Silvija Bilokapić / Ingmar B Schäfer / Mario Halić / Nikolina Sekulić /
Abstract: Centromeres are defined epigenetically by nucleosomes containing the histone H3 variant CENP-A, upon which the constitutive centromere-associated network of proteins (CCAN) is built. CENP-C is ...Centromeres are defined epigenetically by nucleosomes containing the histone H3 variant CENP-A, upon which the constitutive centromere-associated network of proteins (CCAN) is built. CENP-C is considered to be a central organizer of the CCAN. We provide new molecular insights into the structure of human CENP-A nucleosomes, in isolation and in complex with the CENP-C central region (CENP-C ), the main CENP-A binding module of human CENP-C. We establish that the short αN helix of CENP-A promotes DNA flexibility at the nucleosome ends, independently of the sequence it wraps. Furthermore, we show that, in vitro, two regions of human CENP-C (CENP-C and CENP-C ) both bind exclusively to the CENP-A nucleosome. We find CENP-C to bind with high affinity due to an extended hydrophobic area made up of CENP-A and CENP-A . Importantly, we identify two key conformational changes within the CENP-A nucleosome upon CENP-C binding. First, the loose DNA wrapping of CENP-A nucleosomes is further exacerbated, through destabilization of the H2A C-terminal tail. Second, CENP-C rigidifies the N-terminal tail of H4 in the conformation favoring H4 monomethylation, essential for a functional centromere.
History
DepositionJul 30, 2019-
Header (metadata) releaseAug 14, 2019-
Map releaseAug 14, 2019-
UpdateOct 16, 2019-
Current statusOct 16, 2019Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.0092
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.0092
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_10159.png

Downloads & links

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Map

FileDownload / File: emd_10159.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 240 pix.
= 254.4 Å		1.06 Å/pix.
x 240 pix.
= 254.4 Å		1.06 Å/pix.
x 240 pix.
= 254.4 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.06 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0092 / Movie #1: 0.0092
Minimum - Maximum-0.01074206 - 0.038769398
Average (Standard dev.)0.0002594722 (±0.0019139643)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions240240240
Spacing240240240
CellA=B=C: 254.4 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.061.061.06
M x/y/z240240240
origin x/y/z0.0000.0000.000
length x/y/z254.400254.400254.400
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS240240240
D min/max/mean-0.0110.0390.000

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Supplemental data

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Sample components

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Entire Class 1C : CENP-A nucleosome

EntireName: Class 1C : CENP-A nucleosome / Number of components: 1

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Component #1: protein, Class 1C : CENP-A nucleosome

ProteinName: Class 1C : CENP-A nucleosome / Recombinant expression: No

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Experimental details

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Sample preparation

SpecimenSpecimen state: Particle / Method: cryo EM
Sample solutionSpecimen conc.: 1.2 mg/mL / pH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
ImagingMicroscope: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 100 e/Å2 / Illumination mode: FLOOD BEAM
LensImaging mode: BRIGHT FIELD
Specimen HolderModel: OTHER
CameraDetector: GATAN K2 SUMMIT (4k x 4k)

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Image processing

ProcessingMethod: single particle reconstruction / Applied symmetry: C1 (asymmetric) / Number of projections: 104000
3D reconstructionResolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF

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