8u8c

Crystal structure of the TREX-2 complex in complex with the N-terminal motif of Sub2

Method: X-RAY DIFFRACTION Dmax: 109.6 Å Quality: EXCELLENT

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

Nuclear mRNA export protein SAC3

Saccharomyces cerevisiae S288C

UniProt P46674

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 60–551 Not recorded Nuclear mRNA export protein THP1 × 1 (Q08231) 26S proteasome complex subunit SEM1 × 1 (O94742) ATP-dependent RNA helicase SUB2 × 1 (Q07478) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.1 M MES, pH 6.5, and 20% PEG3350 Resolution 2.40 Å R-free 0.231

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.

8 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SAC3_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–497; UniProt 60–551

Nuclear mRNA export protein THP1

Saccharomyces cerevisiae S288C

UniProt Q08231

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–455 Not recorded Nuclear mRNA export protein SAC3 × 1 (P46674) 26S proteasome complex subunit SEM1 × 1 (O94742) ATP-dependent RNA helicase SUB2 × 1 (Q07478) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.1 M MES, pH 6.5, and 20% PEG3350 Resolution 2.40 Å R-free 0.231

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.

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

View Construct and Data Evidence
UniProt name THP1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–455; UniProt 1–455

26S proteasome complex subunit SEM1

Saccharomyces cerevisiae S288C

UniProt O94742

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–89 Not recorded Nuclear mRNA export protein SAC3 × 1 (P46674) Nuclear mRNA export protein THP1 × 1 (Q08231) ATP-dependent RNA helicase SUB2 × 1 (Q07478) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.1 M MES, pH 6.5, and 20% PEG3350 Resolution 2.40 Å R-free 0.231

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.

35 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEM1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–89; UniProt 1–89

ATP-dependent RNA helicase SUB2

Saccharomyces cerevisiae S288C

UniProt Q07478

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–55 Not recorded Nuclear mRNA export protein SAC3 × 1 (P46674) Nuclear mRNA export protein THP1 × 1 (Q08231) 26S proteasome complex subunit SEM1 × 1 (O94742) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.1 M MES, pH 6.5, and 20% PEG3350 Resolution 2.40 Å R-free 0.231

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.

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

View Construct and Data Evidence
UniProt name SUB2_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–55; UniProt 1–55

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 8u8c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8u8c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8u8c
Deposition date deposition_date2023-09-17
Structure title titleCrystal structure of the TREX-2 complex in complex with the N-terminal motif of Sub2
Keywords keywordsmRNA binding protein, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.34
Radius of gyration Rg (electron density) rg_electron33.52
Forward intensity I(0) i0183904000.00
Molecular weight molecular_weight110760.0 kDa
Excluded volume excluded_volume139450 ų
Envelope volume envelope_volume174400 ų
Hydration-shell volume shell_volume43185 ų
Envelope diameter envelope_diameter108.1
Shell Rg shell_rg40.32
Envelope Rg envelope_rg33.34
Shape Rg shape_rg33.49
Total Rg total_rg34.12
Total atoms total_atoms7806
Residues n_residues948
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 dmax109.6
Rg (real space) rg_real34.27
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real1.8390e+08
I(0) uncertainty (real space) i0_real_error3.2510e+06
Rg (reciprocal space) rg_reciprocal34.32
I(0) (reciprocal space) i0_reciprocal183900000.0000
Solution quality estimate total_estimate0.9068
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.5
Skewness Skewness skewness0.198
Kurtosis Kurtosis kurtosis-0.630
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha50010000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.942

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)