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- EMDB-9802: Nucleosome bound to C-terminal ELYS fragment -

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Basic information

Entry
Database: EMDB / ID: EMD-9802
TitleNucleosome bound to C-terminal ELYS fragment
Map dataThe structure of the nucleosome bound to C-terminal ELYS fragment.
Sample
  • Complex: Nucleosome bound to C-terminal ELYS fragment
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.3 Å
AuthorsKobayashi W / Takizawa Y / Aihara M / Negishi L / Ishii H / Kurumizaka H
CitationJournal: Commun Biol / Year: 2019
Title: Structural and biochemical analyses of the nuclear pore complex component ELYS identify residues responsible for nucleosome binding.
Authors: Wataru Kobayashi / Yoshimasa Takizawa / Maya Aihara / Lumi Negishi / Hajime Ishii / Hitoshi Kurumizaka /
Abstract: The nuclear pore complex embedded within the nuclear envelope is the essential architecture for trafficking macromolecules, such as proteins and RNAs, between the cytoplasm and nucleus. The nuclear ...The nuclear pore complex embedded within the nuclear envelope is the essential architecture for trafficking macromolecules, such as proteins and RNAs, between the cytoplasm and nucleus. The nuclear pore complex assembly occurs on chromatin in the post-mitotic phase of the cell cycle. ELYS (MEL-28/AHCTF1) binds to the nucleosome, which is the basic chromatin unit, and promotes assembly of the complex around the chromosomes in cells. Here we show that the Arg-Arg-Lys (RRK) stretch of the C-terminal ELYS region plays an essential role in the nucleosome binding. The cryo-EM structure and the crosslinking mass spectrometry reveal that the ELYS C-terminal region directly binds to the acidic patch of the nucleosome. These results provide mechanistic insight into the ELYS-nucleosome interaction, which promotes the post-mitotic nuclear pore complex formation around chromosomes in cells.
History
DepositionFeb 1, 2019-
Header (metadata) releaseMay 15, 2019-
Map releaseMay 15, 2019-
UpdateMay 22, 2019-
Current statusMay 22, 2019Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 3.7
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 3.7
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_9802.png

Downloads & links

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Map

FileDownload / File: emd_9802.map.gz / Format: CCP4 / Size: 15.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationThe structure of the nucleosome bound to C-terminal ELYS fragment.
Voxel sizeX=Y=Z: 1.32 Å
Density
Contour LevelBy AUTHOR: 3.7 / Movie #1: 3.7
Minimum - Maximum-14.577457000000001 - 24.215945999999999
Average (Standard dev.)-0.000000001179911 (±0.99999994)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions160160160
Spacing160160160
CellA=B=C: 211.20001 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.321.321.32
M x/y/z160160160
origin x/y/z0.0000.0000.000
length x/y/z211.200211.200211.200
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ513513513
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS160160160
D min/max/mean-14.57724.216-0.000

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Supplemental data

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Sample components

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Entire : Nucleosome bound to C-terminal ELYS fragment

EntireName: Nucleosome bound to C-terminal ELYS fragment
Components
  • Complex: Nucleosome bound to C-terminal ELYS fragment

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Supramolecule #1: Nucleosome bound to C-terminal ELYS fragment

SupramoleculeName: Nucleosome bound to C-terminal ELYS fragment / type: complex / ID: 1 / Parent: 0
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli (E. coli)
Recombinant plasmid: pGEX6P-1-xELYS(2299-2408), pET15b-H3.1, pET15b-H4, pET15b-H2A, pET15b-H2B, pGEM-T-Easy-(Widom 601 145 base-pair)

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TALOS ARCTICA
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: OTHER / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm
Sample stageCooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Digitization - Frames/image: 1-40 / Number grids imaged: 1 / Number real images: 2408 / Average exposure time: 10.0 sec. / Average electron dose: 1.4 e/Å2
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 1300821
CTF correctionSoftware - Name: CTFFIND (ver. 4.1.9)
Startup modelType of model: OTHER / Details: ab initio model calculated by RELION.
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 2.1)
Final 3D classificationNumber classes: 8 / Software - Name: RELION (ver. 2.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 2.1)
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 4.3 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0) / Number images used: 81088
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementProtocol: RIGID BODY FIT

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