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- PDB-8r7n: Overall structure of the U11 snRNP -

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Basic information

Entry
Database: PDB / ID: 8r7n
TitleOverall structure of the U11 snRNP
Components
  • (Small nuclear ribonucleoprotein ...) x 6
  • (U11/U12 small nuclear ribonucleoprotein ...) x 3
  • Programmed cell death protein 7
  • Small nuclear ribonucleoprotein-associated proteins B and B'
  • U11 snRNA
  • Zinc finger matrin-type protein 5
KeywordsSPLICING / minor spliceosome / U11 snRNP / RNA-protein complex
Function / homology
Function and homology information


U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / U7 snRNP / snRNA binding / histone pre-mRNA 3'end processing complex / SLBP independent Processing of Histone Pre-mRNAs / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs / protein methylation / U12-type spliceosomal complex ...U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / U7 snRNP / snRNA binding / histone pre-mRNA 3'end processing complex / SLBP independent Processing of Histone Pre-mRNAs / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs / protein methylation / U12-type spliceosomal complex / 7-methylguanosine cap hypermethylation / U1 snRNP binding / methylosome / pICln-Sm protein complex / snRNP binding / small nuclear ribonucleoprotein complex / SMN-Sm protein complex / spliceosomal tri-snRNP complex / P granule / telomerase holoenzyme complex / U2-type precatalytic spliceosome / commitment complex / telomerase RNA binding / U2-type spliceosomal complex / U2-type prespliceosome assembly / U2-type catalytic step 2 spliceosome / RNA Polymerase II Transcription Termination / U2 snRNP / U1 snRNP / U4 snRNP / U2-type prespliceosome / precatalytic spliceosome / spliceosomal complex assembly / mRNA Splicing - Minor Pathway / U5 snRNP / spliceosomal snRNP assembly / U4/U6 x U5 tri-snRNP complex / intercellular bridge / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / RNA splicing / response to glucocorticoid / spliceosomal complex / mRNA splicing, via spliceosome / mRNA processing / snRNP Assembly / SARS-CoV-2 modulates host translation machinery / nuclear body / mRNA binding / apoptotic process / nucleolus / enzyme binding / RNA binding / extracellular exosome / zinc ion binding / nucleoplasm / nucleus / cytoplasm / cytosol
Similarity search - Function
Programmed cell death protein 7 / snRNP35, RNA recognition motif / : / Programmed cell death protein 7 / U11/U12 small nuclear ribonucleoprotein 25kDa protein / SNRNP25, ubiquitin-like domain / Ubiquitin-like domain / : / TRM13/UPF0224 family, U11-48K-like CHHC zinc finger domain / U11-48K-like CHHC zinc finger ...Programmed cell death protein 7 / snRNP35, RNA recognition motif / : / Programmed cell death protein 7 / U11/U12 small nuclear ribonucleoprotein 25kDa protein / SNRNP25, ubiquitin-like domain / Ubiquitin-like domain / : / TRM13/UPF0224 family, U11-48K-like CHHC zinc finger domain / U11-48K-like CHHC zinc finger / Zinc finger CHHC U11-48K-type profile. / : / U1-C, C2H2-type zinc finger / U1 zinc finger / Zinc finger C-x8-C-x5-C-x3-H type (and similar) / Small ribonucleoprotein associated, SmB/SmN / Small nuclear ribonucleoprotein D1 / Zinc finger, CCCH-type superfamily / zinc finger / Small nuclear ribonucleoprotein Sm D3 / Small nuclear ribonucleoprotein Sm D2 / Small nuclear ribonucleoprotein E / Small nuclear ribonucleoprotein G / Small nuclear ribonucleoprotein F / Sm-like protein Lsm7/SmG / Like-Sm (LSM) domain containing protein, LSm4/SmD1/SmD3 / Sm-like protein Lsm6/SmF / Zinc finger, CCCH-type / Zinc finger C3H1-type profile. / LSM domain / LSM domain, eukaryotic/archaea-type / snRNP Sm proteins / : / Sm domain profile. / LSM domain superfamily / Zinc finger C2H2 superfamily / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / Nucleotide-binding alpha-beta plait domain superfamily
Similarity search - Domain/homology
: / RNA / RNA (> 10) / RNA (> 100) / Small nuclear ribonucleoprotein-associated proteins B and B' / Small nuclear ribonucleoprotein E / Small nuclear ribonucleoprotein F / Small nuclear ribonucleoprotein G / Small nuclear ribonucleoprotein Sm D1 / Small nuclear ribonucleoprotein Sm D2 ...: / RNA / RNA (> 10) / RNA (> 100) / Small nuclear ribonucleoprotein-associated proteins B and B' / 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 / U11/U12 small nuclear ribonucleoprotein 35 kDa protein / U11/U12 small nuclear ribonucleoprotein 48 kDa protein / Programmed cell death protein 7 / U11/U12 small nuclear ribonucleoprotein 25 kDa protein / Zinc finger matrin-type protein 5
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsZhao, J. / Galej, W.P.
Funding supportEuropean Union, 1items
OrganizationGrant numberCountry
European Research Council (ERC)950278European Union
CitationJournal: Mol Cell / Year: 2025
Title: Structural basis of 5' splice site recognition by the minor spliceosome.
Authors: Jiangfeng Zhao / Daniel Peter / Irina Brandina / Xiangyang Liu / Wojciech P Galej /
Abstract: The minor spliceosome catalyzes excision of U12-dependent introns from precursors of eukaryotic messenger RNAs (pre-mRNAs). This process is critical for many cellular functions, but the underlying ...The minor spliceosome catalyzes excision of U12-dependent introns from precursors of eukaryotic messenger RNAs (pre-mRNAs). This process is critical for many cellular functions, but the underlying molecular mechanisms remain elusive. Here, we report a cryoelectron microscopy (cryo-EM) reconstruction of the 13-subunit human U11 small nuclear ribonucleoprotein particle (snRNP) complex in apo and substrate-bound forms, revealing the architecture of the U11 small nuclear RNA (snRNA), five minor spliceosome-specific factors, and the mechanism of the U12-type 5' splice site (5'SS) recognition. SNRNP25 and SNRNP35 specifically recognize U11 snRNA, while PDCD7 bridges SNRNP25 and SNRNP48, located at the distal ends of the particle. SNRNP48 and ZMAT5 are positioned near the 5' end of U11 snRNA and stabilize binding of the incoming 5'SS. Recognition of the U12-type 5'SS is achieved through base-pairing to the 5' end of the U11 snRNA and unexpected, non-canonical base-triple interactions with the U11 snRNA stem-loop 3. Our structures provide mechanistic insights into U12-dependent intron recognition and the evolution of the splicing machinery.
History
DepositionNov 26, 2023Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 5, 2025Provider: repository / Type: Initial release
Revision 1.1Feb 19, 2025Group: Data collection / Database references / Category: citation / em_admin
Item: _citation.journal_volume / _citation.page_first / _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: U11 snRNA
B: U11/U12 small nuclear ribonucleoprotein 25 kDa protein
C: U11/U12 small nuclear ribonucleoprotein 35 kDa protein
D: Programmed cell death protein 7
E: Zinc finger matrin-type protein 5
F: U11/U12 small nuclear ribonucleoprotein 48 kDa protein
h: Small nuclear ribonucleoprotein Sm D1
i: Small nuclear ribonucleoprotein Sm D2
j: Small nuclear ribonucleoprotein Sm D3
k: Small nuclear ribonucleoprotein-associated proteins B and B'
l: Small nuclear ribonucleoprotein E
m: Small nuclear ribonucleoprotein F
n: Small nuclear ribonucleoprotein G


Theoretical massNumber of molelcules
Total (without water)297,65313
Polymers297,65313
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

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RNA chain , 1 types, 1 molecules A

#1: RNA chain U11 snRNA


Mass: 43505.629 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 161169046

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U11/U12 small nuclear ribonucleoprotein ... , 3 types, 3 molecules BCF

#2: Protein U11/U12 small nuclear ribonucleoprotein 25 kDa protein / U11/U12 snRNP 25 kDa protein / U11/U12-25K / Minus-99 protein


Mass: 15290.729 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BV90
#3: Protein U11/U12 small nuclear ribonucleoprotein 35 kDa protein / U11/U12 snRNP 35 kDa protein / U11/U12-35K / Protein HM-1 / U1 snRNP-binding protein homolog


Mass: 29514.471 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q16560
#6: Protein U11/U12 small nuclear ribonucleoprotein 48 kDa protein / U11/U12 snRNP 48 kDa protein / U11/U12-48K


Mass: 40042.621 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q6IEG0

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Protein , 3 types, 3 molecules DEk

#4: Protein Programmed cell death protein 7 / ES18 / hES18


Mass: 54791.984 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q8N8D1
#5: Protein Zinc finger matrin-type protein 5 / U11/U12 small nuclear ribonucleoprotein 20 kDa protein / U11/U12 snRNP 20 kDa protein / U11/U12-20K


Mass: 20002.801 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9UDW3
#10: Protein Small nuclear ribonucleoprotein-associated proteins B and B' / snRNP-B / Sm protein B/B' / SmB/B'


Mass: 24642.131 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P14678

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Small nuclear ribonucleoprotein ... , 6 types, 6 molecules hijlmn

#7: Protein Small nuclear ribonucleoprotein Sm D1 / Sm-D1 / Sm-D autoantigen / snRNP core protein D1


Mass: 13310.653 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62314
#8: Protein Small nuclear ribonucleoprotein Sm D2 / Sm-D2 / snRNP core protein D2


Mass: 13551.928 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62316
#9: Protein Small nuclear ribonucleoprotein Sm D3 / Sm-D3 / snRNP core protein D3


Mass: 13940.308 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62318
#11: Protein Small nuclear ribonucleoprotein E / snRNP-E / Sm protein E / SmE


Mass: 10817.601 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62304
#12: Protein Small nuclear ribonucleoprotein F / snRNP-F / Sm protein F / SmF


Mass: 9734.171 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62306
#13: Protein Small nuclear ribonucleoprotein G / snRNP-G / Sm protein G / SmG


Mass: 8508.084 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62308

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Details

Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Overall structure of the apo-U11 snRNP / Type: COMPLEX / Entity ID: all / Source: NATURAL
Molecular weightValue: 0.3 MDa / Experimental value: NO
Source (natural)Organism: Homo sapiens (human)
Buffer solutionpH: 7.9 / Details: 20 mM HEPES-KOH, pH 7.9 200 mM KCl 2 mM MgCl2
Buffer component
IDConc.NameFormulaBuffer-ID
1200 mMpotassium chlorideKCl1
22 mMmagnesium chlorideMgCl21
SpecimenConc.: 0.2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: This sample was monodisperse
Specimen supportGrid material: GOLD / Grid mesh size: 200 divisions/in. / Grid type: UltrAuFoil R2/2
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 95 % / Chamber temperature: 277.15 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Details: Preliminary grid screening was performed on Glacios.
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 165000 X / Nominal defocus max: 1700 nm / Nominal defocus min: 700 nm / Cs: 2.7 mm / C2 aperture diameter: 50 µm / Alignment procedure: ZEMLIN TABLEAU
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 41.73 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) / Num. of grids imaged: 2 / Num. of real images: 30164 / Details: Images were colleted in EER format
EM imaging opticsEnergyfilter name: TFS Selectris X / Energyfilter slit width: 20 eV
Image scansWidth: 4096 / Height: 4096

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Processing

EM software
IDNameVersionCategory
1cryoSPARCv4.3.1particle selection
2SerialEMimage acquisition
7UCSF ChimeraX1.6.1model fitting
9cryoSPARCv4.3.1initial Euler assignment
10cryoSPARCv4.3.1final Euler assignment
11cryoSPARCv4.3.1classification
12cryoSPARCv4.3.13D reconstruction
13PHENIX1.20.1model refinement
CTF correctionType: NONE
Particle selectionNum. of particles selected: 7144222 / Details: Topaz picking is performed with user-trained model
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 222666 / Symmetry type: POINT
Atomic model buildingB value: 71.2 / Protocol: RIGID BODY FIT / Space: REAL / Target criteria: Cross-correction coefficient / Details: refinement is done in Phenix
Atomic model building

3D fitting-ID: 1

IDPDB-IDPdb chain-IDAccession codeChain-IDChain residue rangeInitial refinement model-IDSource nameTypePdb chain residue range
1AF-Q9BV90-F1B1-1321AlphaFoldin silico model
2AF-Q16560-F1C1-2462AlphaFoldin silico model
3AF-Q8N8D1-F1D1-4853AlphaFoldin silico model
4AF-Q9UDW3-F1E1-1704AlphaFoldin silico model
5AF-Q6IEG0-F1F1-3395AlphaFoldin silico model
64PJO

4pjo

i4PJOi11-1146PDBexperimental model11-114
74PJO

4pjo

m4PJOm2-756PDBexperimental model2-75
84PJO

4pjo

l4PJOl14-906PDBexperimental model14-90
94PJO

4pjo

n4PJOn4-766PDBexperimental model4-76
104PJO

4pjo

j4PJOj3-836PDBexperimental model3-83
114PJO

4pjo

k4PJOk6-916PDBexperimental model6-91
124PJO

4pjo

h4PJOh2-826PDBexperimental model2-82

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