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- EMDB-4240: Human Bact spliceosome state 8 unmasked -

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Basic information

Entry
Database: EMDB / ID: EMD-4240
TitleHuman Bact spliceosome state 8 unmasked
Map data
Sample
  • Complex: human Bact spliceosome state 1 unmasked
Function / homology
Function and homology information


RES complex / negative regulation of chemokine-mediated signaling pathway / regulation of vitamin D receptor signaling pathway / regulation of retinoic acid receptor signaling pathway / U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / U7 snRNP / generation of catalytic spliceosome for first transesterification step / 3'-5' RNA helicase activity ...RES complex / negative regulation of chemokine-mediated signaling pathway / regulation of vitamin D receptor signaling pathway / regulation of retinoic acid receptor signaling pathway / U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / U7 snRNP / generation of catalytic spliceosome for first transesterification step / 3'-5' RNA helicase activity / cis assembly of pre-catalytic spliceosome / histone pre-mRNA 3'end processing complex / U4atac snRNP / SLBP independent Processing of Histone Pre-mRNAs / nuclear histone mRNA catabolic process / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs / U4atac/U6atac snRNP / B-WICH complex / C2H2 zinc finger domain binding / U11/U12 snRNP / poly(A) binding / miRNA processing / U4atac/U6atac x U5 tri-snRNP complex / 7-methylguanosine cap hypermethylation / U12-type spliceosomal complex / embryonic brain development / U1 snRNP binding / regulation of mRNA splicing, via spliceosome / nuclear retinoic acid receptor binding / positive regulation of mRNA splicing, via spliceosome / RNA splicing, via transesterification reactions / pICln-Sm protein complex / snRNP binding / RNA Polymerase II Transcription Termination / mRNA 3'-end processing / sno(s)RNA-containing ribonucleoprotein complex / methylosome / splicing factor binding / small nuclear ribonucleoprotein complex / U12-type catalytic step 2 spliceosome / post-spliceosomal complex / SMN-Sm protein complex / spliceosomal tri-snRNP complex / positive regulation of vitamin D receptor signaling pathway / U12-type precatalytic spliceosome / P granule / commitment complex / host-mediated activation of viral transcription / U2-type precatalytic spliceosome / post-mRNA release spliceosomal complex / Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells / RUNX3 regulates NOTCH signaling / Notch binding / U2-type spliceosomal complex / telomerase holoenzyme complex / nuclear vitamin D receptor binding / Transport of Mature mRNA derived from an Intron-Containing Transcript / U2-type prespliceosome assembly / telomerase RNA binding / NOTCH4 Intracellular Domain Regulates Transcription / pre-mRNA binding / U4/U6 snRNP / U2-type catalytic step 2 spliceosome / positive regulation of neurogenesis / SAGA complex / protein methylation / U1 snRNP / spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) / U2 snRNP / NOTCH3 Intracellular Domain Regulates Transcription / U4 snRNP / mRNA stabilization / U2-type prespliceosome / U2-type catalytic step 1 spliceosome / RHOBTB1 GTPase cycle / protein peptidyl-prolyl isomerization / cyclosporin A binding / nuclear androgen receptor binding / K63-linked polyubiquitin modification-dependent protein binding / generation of catalytic spliceosome for second transesterification step / ubiquitin-ubiquitin ligase activity / Notch-HLH transcription pathway / Formation of paraxial mesoderm / pattern recognition receptor activity / positive regulation of transforming growth factor beta receptor signaling pathway / regulation of RNA splicing / mRNA 3'-splice site recognition / WD40-repeat domain binding / SMAD binding / positive regulation of transcription by RNA polymerase III / mRNA Splicing - Minor Pathway / spliceosomal complex assembly / positive regulation of transcription by RNA polymerase I / precatalytic spliceosome / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / Prp19 complex / U2 snRNA binding / negative regulation of mRNA splicing, via spliceosome / U5 snRNA binding / spliceosomal tri-snRNP complex assembly
Similarity search - Function
: / : / Pre-mRNA-splicing factor CWC24-like / Ist3-like, RNA recognition motif / : / Bud13 / : / Pre-mRNA-splicing factor of RES complex / : / Pre-mRNA-splicing factor Isy1 ...: / : / Pre-mRNA-splicing factor CWC24-like / Ist3-like, RNA recognition motif / : / Bud13 / : / Pre-mRNA-splicing factor of RES complex / : / Pre-mRNA-splicing factor Isy1 / Pre-mRNA-splicing factor Isy1 superfamily / Isy1-like splicing family / Prp19 WD40 domain / : / : / : / : / Intron-binding protein aquarius, beta-barrel / Intron-binding protein aquarius insert domain / RBM22 CCCH zinc finger domain / Peptidyl-prolyl cis-trans isomerase E / PWI domain superfamily / PWI domain / PWI domain profile. / SF3B6, RNA recognition motif / Peptidyl-prolyl cis-trans isomerase E, RNA recognition motif / Pre-mRNA-splicing factor SPF27 / Breast carcinoma amplified sequence 2 (BCAS2) / CWF11 family / Intron-binding protein aquarius, N-terminal / Intron-binding protein aquarius N-terminal / Splicing factor SF3a60 binding domain / Splicing factor SF3a60 binding domain / PWI domain / PWI, domain in splicing factors / Splicing factor 3A subunit 1, ubiquitin domain / Helix hairpin bin domain superfamily / U2 small nuclear ribonucleoprotein B'', RNA recognition motif 2 / U2 small nuclear ribonucleoprotein B'', RNA recognition motif 1 / : / : / Replication stress response SDE2 C-terminal / : / Cactus-binding C-terminus of cactin protein / SF3A2 domain / : / Pre-mRNA-splicing factor SF3a complex subunit 2 (Prp11) / cwf21 domain / Splicing factor SF3a60 /Prp9 subunit, C-terminal / SF3A3 domain / SF3a60/Prp9 C-terminal / Pre-mRNA-splicing factor SF3A3, of SF3a complex, Prp9 / mRNA splicing factor Cwf21 domain / Splicing factor 3A subunit 1, conserved domain / Splicing factor 3A subunit 1 / Pre-mRNA splicing factor PRP21 like protein / Zinc finger C-x8-C-x5-C-x3-H type (and similar) / Pre-mRNA-processing factor 17 / G10 protein signature 2. / : / : / Pre-mRNA-splicing factor SYF1 middle HAT repeat / : / Domain of unknown function DUF382 / Domain of unknown function (DUF382) / SWAP/Surp / Pre-mRNA-splicing factor 19 / SWAP/Surp superfamily / Pre-mRNA-processing factor 19 / : / Surp module / Prp19/Pso4-like / SURP motif repeat profile. / Suppressor-of-White-APricot splicing regulator / BUD31/G10-related, conserved site / G10 protein signature 1. / Splicing factor 3B, subunit 5 / : / STL11, N-terminal / Splicing factor 3B subunit 1 / Splicing factor 3B subunit 1 / Zinc-finger of C2H2 type / Cyclophilin-type peptidyl-prolyl cis-trans isomerase, cyclophilin A-like / : / Pre-mRNA-splicing factor Syf1/CRNKL1 C-terminal HAT repeat / PSP, proline-rich / Pre-mRNA-splicing factor Cwc2/Slt11 / PSP / UPF1-type helicase core domain profile. / proline-rich domain in spliceosome associated proteins / SKI-interacting protein SKIP, SNW domain / Pre-mRNA-splicing factor Cwf15/Cwc15 / SKI-interacting protein, SKIP / SKIP/SNW domain / Cwf15/Cwc15 cell cycle control protein / U-box domain / Matrin/U1-C, C2H2-type zinc finger / WD repeat Prp46/PLRG1-like / Zinc finger matrin-type profile. / Pre-mRNA splicing factor component Cdc5p/Cef1, C-terminal
Similarity search - Domain/homology
E3 ubiquitin-protein ligase RNF113A / Pleiotropic regulator 1 / Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16 / RNA helicase aquarius / Pre-mRNA-processing factor 17 / Splicing factor 3B subunit 1 / U5 small nuclear ribonucleoprotein 200 kDa helicase / Pre-mRNA-splicing factor SPF27 / U2 small nuclear ribonucleoprotein B'' / U2 small nuclear ribonucleoprotein A' ...E3 ubiquitin-protein ligase RNF113A / Pleiotropic regulator 1 / Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16 / RNA helicase aquarius / Pre-mRNA-processing factor 17 / Splicing factor 3B subunit 1 / U5 small nuclear ribonucleoprotein 200 kDa helicase / Pre-mRNA-splicing factor SPF27 / U2 small nuclear ribonucleoprotein B'' / U2 small nuclear ribonucleoprotein A' / Small nuclear ribonucleoprotein-associated proteins B and B' / Protein BUD31 homolog / Small nuclear ribonucleoprotein E / Small nuclear ribonucleoprotein F / Small nuclear ribonucleoprotein G / Small nuclear ribonucleoprotein Sm D1 / Small nuclear ribonucleoprotein Sm D2 / Small nuclear ribonucleoprotein Sm D3 / Splicing factor 3A subunit 3 / Splicing factor 3B subunit 2 / SNW domain-containing protein 1 / 116 kDa U5 small nuclear ribonucleoprotein component / Splicing factor 3B subunit 3 / Splicing factor 3A subunit 2 / Splicing factor 3A subunit 1 / Pre-mRNA-processing-splicing factor 8 / Spliceosome-associated protein CWC27 homolog / PHD finger-like domain-containing protein 5A / Serine/arginine repetitive matrix protein 1 / Smad nuclear-interacting protein 1 / U5 small nuclear ribonucleoprotein 40 kDa protein / Cell division cycle 5-like protein / BUD13 homolog / Splicing factor 3B subunit 5 / Crooked neck-like protein 1 / Pre-mRNA-splicing factor CWC22 homolog / Pre-mRNA-splicing factor SYF1 / Pre-mRNA-splicing factor RBM22 / Spliceosome-associated protein CWC15 homolog / Pre-mRNA-splicing factor ISY1 homolog / Pre-mRNA-processing factor 19 / Peptidyl-prolyl cis-trans isomerase E / Serine/arginine repetitive matrix protein 2 / RNA-binding motif protein, X-linked 2 / Splicing factor 3B subunit 6 / Peptidyl-prolyl cis-trans isomerase-like 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.5 Å
AuthorsHaselbach D / Komarov I / Agafonov D / Kastner B / Luehrmann R / Stark H
CitationJournal: Cell / Year: 2018
Title: Structure and Conformational Dynamics of the Human Spliceosomal B Complex.
Authors: David Haselbach / Ilya Komarov / Dmitry E Agafonov / Klaus Hartmuth / Benjamin Graf / Olexandr Dybkov / Henning Urlaub / Berthold Kastner / Reinhard Lührmann / Holger Stark /
Abstract: The spliceosome is a highly dynamic macromolecular complex that precisely excises introns from pre-mRNA. Here we report the cryo-EM 3D structure of the human B spliceosome at 3.4 Å resolution. In ...The spliceosome is a highly dynamic macromolecular complex that precisely excises introns from pre-mRNA. Here we report the cryo-EM 3D structure of the human B spliceosome at 3.4 Å resolution. In the B state, the spliceosome is activated but not catalytically primed, so that it is functionally blocked prior to the first catalytic step of splicing. The spliceosomal core is similar to the yeast B spliceosome; important differences include the presence of the RNA helicase aquarius and peptidyl prolyl isomerases. To examine the overall dynamic behavior of the purified spliceosome, we developed a principal component analysis-based approach. Calculating the energy landscape revealed eight major conformational states, which we refined to higher resolution. Conformational differences of the highly flexible structural components between these eight states reveal how spliceosomal components contribute to the assembly of the spliceosome, allowing it to generate a dynamic interaction network required for its subsequent catalytic activation.
History
DepositionDec 22, 2017-
Header (metadata) releaseFeb 7, 2018-
Map releaseFeb 7, 2018-
UpdateFeb 7, 2018-
Current statusFeb 7, 2018Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.013
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.013
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6ff7
  • Surface level: 0.013
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_4240.png

Downloads & links

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Map

FileDownload / File: emd_4240.map.gz / Format: CCP4 / Size: 282.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.16 Å/pix.
x 420 pix.
= 487.2 Å		1.16 Å/pix.
x 420 pix.
= 487.2 Å		1.16 Å/pix.
x 420 pix.
= 487.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.16 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.013 / Movie #1: 0.013
Minimum - Maximum-0.014408626 - 0.06181489
Average (Standard dev.)0.00064544595 (±0.004007307)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions420420420
Spacing420420420
CellA=B=C: 487.19998 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.161.161.16
M x/y/z420420420
origin x/y/z0.0000.0000.000
length x/y/z487.200487.200487.200
α/β/γ90.00090.00090.000
start NX/NY/NZ-128-128-128
NX/NY/NZ256256256
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS420420420
D min/max/mean-0.0140.0620.001

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Supplemental data

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Sample components

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Entire : human Bact spliceosome state 1 unmasked

EntireName: human Bact spliceosome state 1 unmasked
Components
  • Complex: human Bact spliceosome state 1 unmasked

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Supramolecule #1: human Bact spliceosome state 1 unmasked

SupramoleculeName: human Bact spliceosome state 1 unmasked / type: complex / ID: 1 / Parent: 0
Source (natural)Organism: Homo sapiens (human) / Strain: HELA
Molecular weightTheoretical: 4.5 MDa

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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

Concentration0.05 mg/mL
BufferpH: 7.9
Component:
ConcentrationNameFormula
20.0 mMHEPES
150.0 mMNaCl
1.5 mMMgCl2
GridModel: Quantifoil R3.5/1 / Material: COPPER / Mesh: 400 / Support film - #0 - Film type ID: 1 / Support film - #0 - Material: CARBON / Support film - #0 - topology: HOLEY / Support film - #1 - Film type ID: 2 / Support film - #1 - Material: CARBON / Support film - #1 - topology: CONTINUOUS
VitrificationCryogen name: ETHANE / Chamber humidity: 75 % / Chamber temperature: 277 K / Instrument: LEICA EM GP / Details: blot with blotting sensor.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Alignment procedureComa free - Residual tilt: 14.0 mrad
Specialist opticsSpherical aberration corrector: Microscope was modified with a Cs corrector with two hexapoles elements
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Digitization - Sampling interval: 14.0 µm / Number grids imaged: 1 / Number real images: 32000 / Average exposure time: 1.0 sec. / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Cs: 0.001 mm / Nominal defocus max: 4.5 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 59000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 3300000
CTF correctionSoftware - Name: Gctf
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 4.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 2.1) / Number images used: 165853
Initial angle assignmentType: OTHER / Software - Name: EMAN2
Final angle assignmentType: PROJECTION MATCHING / Software - Name: RELION
Final 3D classificationNumber classes: 220 / Software - Name: RELION

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Atomic model buiding 1

RefinementProtocol: RIGID BODY FIT
Output model

PDB-6ff7:
human Bact spliceosome core structure

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