4b0a

The high-resolution structure of yTBP-yTAF1 identifies conserved and competing interaction surfaces in transcriptional activation

Method: X-RAY DIFFRACTION Dmax: 69.3 Å Quality: GOOD

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

TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 1, LINKER, TATA-BOX-BINDING PROTEIN

SACCHAROMYCES CEREVISIAE

UniProt P13393

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 61–240 Fragment:TAF1 RESIDUES 8-71, LINKER, TBP RESIDUE 61-240 Mutation:YES CA CALCIUM ION × 3 GOL GLYCEROL × 6 CL CHLORIDE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.97 Å R-free 0.223

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.

48 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBP_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 99–278; UniProt 61–240

TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 1, LINKER, TATA-BOX-BINDING PROTEIN

SACCHAROMYCES CEREVISIAE

UniProt P46677

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 8–71 Fragment:TAF1 RESIDUES 8-71, LINKER, TBP RESIDUE 61-240 Mutation:YES CA CALCIUM ION × 3 GOL GLYCEROL × 6 CL CHLORIDE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.97 Å R-free 0.223

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 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TAF1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 22–85; UniProt 8–71

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 4b0a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4b0a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4b0a
Deposition date deposition_date2012-06-29
Structure title titleThe high-resolution structure of yTBP-yTAF1 identifies conserved and competing interaction surfaces in transcriptional activation
Keywords keywordsTRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.17
Radius of gyration Rg (electron density) rg_electron20.39
Forward intensity I(0) i012172900.00
Molecular weight molecular_weight26944.0 kDa
Excluded volume excluded_volume34068 ų
Envelope volume envelope_volume40700 ų
Hydration-shell volume shell_volume17491 ų
Envelope diameter envelope_diameter72.4
Shell Rg shell_rg26.06
Envelope Rg envelope_rg20.51
Shape Rg shape_rg20.39
Total Rg total_rg21.25
Total atoms total_atoms1891
Residues n_residues237
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 dmax69.3
Rg (real space) rg_real21.23
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real1.2170e+07
I(0) uncertainty (real space) i0_real_error1.7790e+05
Rg (reciprocal space) rg_reciprocal21.22
I(0) (reciprocal space) i0_reciprocal12170000.0000
Solution quality estimate total_estimate0.8023
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.4
Skewness Skewness skewness0.395
Kurtosis Kurtosis kurtosis-0.444
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2965000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.833; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.927; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4b0aA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology310 — TATA-Binding Protein
Homologous superfamily homologous superfamily10 — TATA-Binding Protein
Domain ID domain_id4b0aA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology310 — TATA-Binding Protein
Homologous superfamily homologous superfamily10 — TATA-Binding Protein

8. Citations (1)

9. Files and Curves (10)