9g8n

80S-bound human Ski2-exosome complex

Method: ELECTRON MICROSCOPY Dmax: 218.5 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Exosome complex component RRP41

Homo sapiens

UniProt Q9NPD3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 12 RNA 1 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain L; UniProt 1–245 Not recorded Exosome complex component RRP43 × 1 (Q96B26) Exosome complex component RRP46 × 1 (Q9NQT4) Exosome complex component RRP42 × 1 (Q15024) Exosome complex component RRP40 × 1 (Q9NQT5) Exosome complex component CSL4 × 1 (Q9Y3B2) CrPV-IRES RNA × 1 Helicase SKI2W × 1 (Q15477) Exosome complex component MTR3 × 1 (Q5RKV6) Exosome complex component RRP4 × 1 (Q13868) Isoform 2 of HBS1-like protein × 1 (Q9Y450) Exosome complex component RRP45 × 1 (Q06265) DIS3-like exonuclease 1 × 1 (Q8TF46) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXOS4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain L; PDBConstruct 1–245; UniProt 1–245

Exosome complex component RRP43

Homo sapiens

UniProt Q96B26

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 12 RNA 1 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain N; UniProt 1–276 Not recorded Exosome complex component RRP41 × 1 (Q9NPD3) Exosome complex component RRP46 × 1 (Q9NQT4) Exosome complex component RRP42 × 1 (Q15024) Exosome complex component RRP40 × 1 (Q9NQT5) Exosome complex component CSL4 × 1 (Q9Y3B2) CrPV-IRES RNA × 1 Helicase SKI2W × 1 (Q15477) Exosome complex component MTR3 × 1 (Q5RKV6) Exosome complex component RRP4 × 1 (Q13868) Isoform 2 of HBS1-like protein × 1 (Q9Y450) Exosome complex component RRP45 × 1 (Q06265) DIS3-like exonuclease 1 × 1 (Q8TF46) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXOS8_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain N; PDBConstruct 5–280; UniProt 1–276

Exosome complex component RRP46

Homo sapiens

UniProt Q9NQT4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 12 RNA 1 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain O; UniProt 1–235 Not recorded Exosome complex component RRP41 × 1 (Q9NPD3) Exosome complex component RRP43 × 1 (Q96B26) Exosome complex component RRP42 × 1 (Q15024) Exosome complex component RRP40 × 1 (Q9NQT5) Exosome complex component CSL4 × 1 (Q9Y3B2) CrPV-IRES RNA × 1 Helicase SKI2W × 1 (Q15477) Exosome complex component MTR3 × 1 (Q5RKV6) Exosome complex component RRP4 × 1 (Q13868) Isoform 2 of HBS1-like protein × 1 (Q9Y450) Exosome complex component RRP45 × 1 (Q06265) DIS3-like exonuclease 1 × 1 (Q8TF46) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXOS5_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain O; PDBConstruct 5–239; UniProt 1–235

Exosome complex component RRP42

Homo sapiens

UniProt Q15024

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 12 RNA 1 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain F; UniProt 1–291 Not recorded Exosome complex component RRP41 × 1 (Q9NPD3) Exosome complex component RRP43 × 1 (Q96B26) Exosome complex component RRP46 × 1 (Q9NQT4) Exosome complex component RRP40 × 1 (Q9NQT5) Exosome complex component CSL4 × 1 (Q9Y3B2) CrPV-IRES RNA × 1 Helicase SKI2W × 1 (Q15477) Exosome complex component MTR3 × 1 (Q5RKV6) Exosome complex component RRP4 × 1 (Q13868) Isoform 2 of HBS1-like protein × 1 (Q9Y450) Exosome complex component RRP45 × 1 (Q06265) DIS3-like exonuclease 1 × 1 (Q8TF46) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXOS7_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 5–295; UniProt 1–291

Exosome complex component RRP40

Homo sapiens

UniProt Q9NQT5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 12 RNA 1 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain H; UniProt 1–275 Not recorded Exosome complex component RRP41 × 1 (Q9NPD3) Exosome complex component RRP43 × 1 (Q96B26) Exosome complex component RRP46 × 1 (Q9NQT4) Exosome complex component RRP42 × 1 (Q15024) Exosome complex component CSL4 × 1 (Q9Y3B2) CrPV-IRES RNA × 1 Helicase SKI2W × 1 (Q15477) Exosome complex component MTR3 × 1 (Q5RKV6) Exosome complex component RRP4 × 1 (Q13868) Isoform 2 of HBS1-like protein × 1 (Q9Y450) Exosome complex component RRP45 × 1 (Q06265) DIS3-like exonuclease 1 × 1 (Q8TF46) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXOS3_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain H; PDBConstruct 5–279; UniProt 1–275

Exosome complex component CSL4

Homo sapiens

UniProt Q9Y3B2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 12 RNA 1 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain J; UniProt 1–195 Not recorded Exosome complex component RRP41 × 1 (Q9NPD3) Exosome complex component RRP43 × 1 (Q96B26) Exosome complex component RRP46 × 1 (Q9NQT4) Exosome complex component RRP42 × 1 (Q15024) Exosome complex component RRP40 × 1 (Q9NQT5) CrPV-IRES RNA × 1 Helicase SKI2W × 1 (Q15477) Exosome complex component MTR3 × 1 (Q5RKV6) Exosome complex component RRP4 × 1 (Q13868) Isoform 2 of HBS1-like protein × 1 (Q9Y450) Exosome complex component RRP45 × 1 (Q06265) DIS3-like exonuclease 1 × 1 (Q8TF46) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXOS1_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain J; PDBConstruct 5–199; UniProt 1–195

Helicase SKI2W

Homo sapiens

UniProt Q15477

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 12 RNA 1 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain A; UniProt 1–1246 Not recorded Exosome complex component RRP41 × 1 (Q9NPD3) Exosome complex component RRP43 × 1 (Q96B26) Exosome complex component RRP46 × 1 (Q9NQT4) Exosome complex component RRP42 × 1 (Q15024) Exosome complex component RRP40 × 1 (Q9NQT5) Exosome complex component CSL4 × 1 (Q9Y3B2) CrPV-IRES RNA × 1 Exosome complex component MTR3 × 1 (Q5RKV6) Exosome complex component RRP4 × 1 (Q13868) Isoform 2 of HBS1-like protein × 1 (Q9Y450) Exosome complex component RRP45 × 1 (Q06265) DIS3-like exonuclease 1 × 1 (Q8TF46) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SKIV2_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain A; PDBConstruct 1–1246; UniProt 1–1246

Exosome complex component MTR3

Homo sapiens

UniProt Q5RKV6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 12 RNA 1 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain G; UniProt 1–272 Not recorded Exosome complex component RRP41 × 1 (Q9NPD3) Exosome complex component RRP43 × 1 (Q96B26) Exosome complex component RRP46 × 1 (Q9NQT4) Exosome complex component RRP42 × 1 (Q15024) Exosome complex component RRP40 × 1 (Q9NQT5) Exosome complex component CSL4 × 1 (Q9Y3B2) CrPV-IRES RNA × 1 Helicase SKI2W × 1 (Q15477) Exosome complex component RRP4 × 1 (Q13868) Isoform 2 of HBS1-like protein × 1 (Q9Y450) Exosome complex component RRP45 × 1 (Q06265) DIS3-like exonuclease 1 × 1 (Q8TF46) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXOS6_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain G; PDBConstruct 1–272; UniProt 1–272

Exosome complex component RRP4

Homo sapiens

UniProt Q13868

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 12 RNA 1 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain I; UniProt 1–293 Not recorded Exosome complex component RRP41 × 1 (Q9NPD3) Exosome complex component RRP43 × 1 (Q96B26) Exosome complex component RRP46 × 1 (Q9NQT4) Exosome complex component RRP42 × 1 (Q15024) Exosome complex component RRP40 × 1 (Q9NQT5) Exosome complex component CSL4 × 1 (Q9Y3B2) CrPV-IRES RNA × 1 Helicase SKI2W × 1 (Q15477) Exosome complex component MTR3 × 1 (Q5RKV6) Isoform 2 of HBS1-like protein × 1 (Q9Y450) Exosome complex component RRP45 × 1 (Q06265) DIS3-like exonuclease 1 × 1 (Q8TF46) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXOS2_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain I; PDBConstruct 5–297; UniProt 1–293

Isoform 2 of HBS1-like protein

Homo sapiens

UniProt Q9Y450

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 12 RNA 1 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain E; UniProt 369–632 Not recorded Exosome complex component RRP41 × 1 (Q9NPD3) Exosome complex component RRP43 × 1 (Q96B26) Exosome complex component RRP46 × 1 (Q9NQT4) Exosome complex component RRP42 × 1 (Q15024) Exosome complex component RRP40 × 1 (Q9NQT5) Exosome complex component CSL4 × 1 (Q9Y3B2) CrPV-IRES RNA × 1 Helicase SKI2W × 1 (Q15477) Exosome complex component MTR3 × 1 (Q5RKV6) Exosome complex component RRP4 × 1 (Q13868) Exosome complex component RRP45 × 1 (Q06265) DIS3-like exonuclease 1 × 1 (Q8TF46) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HBS1L_HUMAN
Isoform Q9Y450-2
PDB entities 11
Chains and sequence ranges Author chain E; PDBConstruct 5–268; UniProt 369–632

Exosome complex component RRP45

Homo sapiens

UniProt Q06265

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 12 RNA 1 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain K; UniProt 1–439 Not recorded Exosome complex component RRP41 × 1 (Q9NPD3) Exosome complex component RRP43 × 1 (Q96B26) Exosome complex component RRP46 × 1 (Q9NQT4) Exosome complex component RRP42 × 1 (Q15024) Exosome complex component RRP40 × 1 (Q9NQT5) Exosome complex component CSL4 × 1 (Q9Y3B2) CrPV-IRES RNA × 1 Helicase SKI2W × 1 (Q15477) Exosome complex component MTR3 × 1 (Q5RKV6) Exosome complex component RRP4 × 1 (Q13868) Isoform 2 of HBS1-like protein × 1 (Q9Y450) DIS3-like exonuclease 1 × 1 (Q8TF46) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EXOS9_HUMAN
Isoform
PDB entities 12
Chains and sequence ranges Author chain K; PDBConstruct 5–443; UniProt 1–439

DIS3-like exonuclease 1

Homo sapiens

UniProt Q8TF46

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 12 RNA 1 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain M; UniProt 1–1054 Not recorded Exosome complex component RRP41 × 1 (Q9NPD3) Exosome complex component RRP43 × 1 (Q96B26) Exosome complex component RRP46 × 1 (Q9NQT4) Exosome complex component RRP42 × 1 (Q15024) Exosome complex component RRP40 × 1 (Q9NQT5) Exosome complex component CSL4 × 1 (Q9Y3B2) CrPV-IRES RNA × 1 Helicase SKI2W × 1 (Q15477) Exosome complex component MTR3 × 1 (Q5RKV6) Exosome complex component RRP4 × 1 (Q13868) Isoform 2 of HBS1-like protein × 1 (Q9Y450) Exosome complex component RRP45 × 1 (Q06265) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DI3L1_HUMAN
Isoform
PDB entities 13
Chains and sequence ranges Author chain M; PDBConstruct 3–1056; UniProt 1–1054

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 9g8n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9g8n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9g8n
Deposition date deposition_date2024-07-23
Structure title title80S-bound human Ski2-exosome complex
Keywords keywordsRibosome, RNase, Helicase, RNA-binding, mRNA-degradation, cytoplasm; RIBOSOME
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier61.18
Radius of gyration Rg (electron density) rg_electron61.83
Forward intensity I(0) i03585910000.00
Molecular weight molecular_weight491260.0 kDa
Excluded volume excluded_volume610950 ų
Envelope volume envelope_volume988150 ų
Hydration-shell volume shell_volume135650 ų
Envelope diameter envelope_diameter248.3
Shell Rg shell_rg61.67
Envelope Rg envelope_rg62.28
Shape Rg shape_rg61.88
Total Rg total_rg61.65
Total atoms total_atoms34405
Residues n_residues4348
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax218.5
Rg (real space) rg_real61.58
Rg uncertainty (real space) rg_real_error1.69
I(0) (real space) i0_real3.5840e+09
I(0) uncertainty (real space) i0_real_error7.6650e+07
Rg (reciprocal space) rg_reciprocal60.78
I(0) (reciprocal space) i0_reciprocal3581000000.0000
Solution quality estimate total_estimate0.8322
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary67.2
Skewness Skewness skewness0.648
Kurtosis Kurtosis kurtosis0.294
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0071
Highest regularization parameter α highest_alpha410500000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.668; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.814

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

8. Citations (1)

9. Files and Curves (10)