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- EMDB-3463: BRCA1-A histone deubiquitinase core complex -

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Basic information

Entry
Database: EMDB / ID: EMD-3463
TitleBRCA1-A histone deubiquitinase core complex
Map dataBRCA1-A histone deubiquitinase core complex
Sample
  • Complex: BRCA1-A histone deubiquitinase core complex
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / negative staining / Resolution: 24.8 Å
AuthorsSmerdon SJ / Rosenthal PB
CitationJournal: Cell Rep / Year: 2016
Title: Three-Dimensional Architecture of the Human BRCA1-A Histone Deubiquitinase Core Complex.
Authors: Otto J P Kyrieleis / Pauline B McIntosh / Sarah R Webb / Lesley J Calder / Janette Lloyd / Nisha A Patel / Stephen R Martin / Carol V Robinson / Peter B Rosenthal / Stephen J Smerdon /
Abstract: BRCA1 is a tumor suppressor found to be mutated in hereditary breast and ovarian cancer and plays key roles in the maintenance of genomic stability by homologous recombination repair. It is recruited ...BRCA1 is a tumor suppressor found to be mutated in hereditary breast and ovarian cancer and plays key roles in the maintenance of genomic stability by homologous recombination repair. It is recruited to damaged chromatin as a component of the BRCA1-A deubiquitinase, which cleaves K63-linked ubiquitin chains attached to histone H2A and H2AX. BRCA1-A contributes to checkpoint regulation, repair pathway choice, and HR repair efficiency through molecular mechanisms that remain largely obscure. The structure of an active core complex comprising two Abraxas/BRCC36/BRCC45/MERIT40 tetramers determined by negative-stain electron microscopy (EM) reveals a distorted V-shape architecture in which a dimer of Abraxas/BRCC36 heterodimers sits at the base, with BRCC45/Merit40 pairs occupying each arm. The location and ubiquitin-binding activity of BRCC45 suggest that it may provide accessory interactions with nucleosome-linked ubiquitin chains that contribute to their efficient processing. Our data also suggest how ataxia telangiectasia mutated (ATM)-dependent BRCA1 dimerization may stabilize self-association of the entire BRCA1-A complex.
History
DepositionNov 10, 2016-
Header (metadata) releaseDec 14, 2016-
Map releaseDec 14, 2016-
UpdateJul 19, 2017-
Current statusJul 19, 2017Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 1.12
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 1.12
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_3463.png

Downloads & links

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Map

FileDownload / File: emd_3463.map.gz / Format: CCP4 / Size: 6.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationBRCA1-A histone deubiquitinase core complex
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
4.3 Å/pix.
x 120 pix.
= 516. Å		4.3 Å/pix.
x 120 pix.
= 516. Å		4.3 Å/pix.
x 120 pix.
= 516. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 4.3 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 1.12 / Movie #1: 1.12
Minimum - Maximum-1.9419398 - 3.765693
Average (Standard dev.)-0.0000522589 (±0.17607792)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions120120120
Spacing120120120
CellA=B=C: 516.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z4.34.34.3
M x/y/z120120120
origin x/y/z0.0000.0000.000
length x/y/z516.000516.000516.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS120120120
D min/max/mean-1.9423.766-0.000

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Supplemental data

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Sample components

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Entire : BRCA1-A histone deubiquitinase core complex

EntireName: BRCA1-A histone deubiquitinase core complex
Components
  • Complex: BRCA1-A histone deubiquitinase core complex

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Supramolecule #1: BRCA1-A histone deubiquitinase core complex

SupramoleculeName: BRCA1-A histone deubiquitinase core complex / type: complex / ID: 1 / Parent: 0
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli (E. coli) / Recombinant plasmid: pET-Duet
Molecular weightExperimental: 600 KDa

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Experimental details

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Structure determination

Methodnegative staining
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.02 mg/mL
BufferpH: 7.5
StainingType: NEGATIVE / Material: 1% phosphotungstate
GridModel: TAAB / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: CONTINUOUS

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Electron microscopy

MicroscopeFEI TECNAI SPIRIT
Image recordingFilm or detector model: FEI EAGLE (2k x 2k) / Digitization - Dimensions - Width: 2048 pixel / Digitization - Dimensions - Height: 2048 pixel / Digitization - Sampling interval: 30.0 µm / Average exposure time: 1.0 sec. / Average electron dose: 30.0 e/Å2
Electron beamAcceleration voltage: 120 kV / Electron source: TUNGSTEN HAIRPIN
Electron opticsC2 aperture diameter: 50.0 µm / Calibrated defocus max: 1.5 µm / Calibrated defocus min: 1.5 µm / Calibrated magnification: 52000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.0 mm / Nominal defocus max: 1.5 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 52000
Sample stageSpecimen holder model: OTHER
Experimental equipment
Model: Tecnai Spirit / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Point group: C2 (2 fold cyclic) / Algorithm: FOURIER SPACE / Resolution.type: BY AUTHOR / Resolution: 24.8 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: FREALIGN / Number images used: 8393
Initial angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: IMAGIC
Final angle assignmentType: PROJECTION MATCHING / Software - Name: FREALIGN
Final 3D classificationNumber classes: 30

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Atomic model buiding 1

RefinementProtocol: RIGID BODY FIT

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