7uqj

Cryo-EM structure of the S. cerevisiae chromatin remodeler Yta7 hexamer bound to ATPgS and histone H3 tail in state II

Method: ELECTRON MICROSCOPY Dmax: 148.5 Å Quality: REASONABLE

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

ATPase histone chaperone YTA7

Saccharomyces cerevisiae

UniProt P40340

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–1379 Chain B; UniProt 1–1379 Chain C; UniProt 1–1379 Chain D; UniProt 1–1379 Chain E; UniProt 1–1379 Chain F; UniProt 1–1379 Not recorded Histone H3 × 1 (P61830) ADP ADENOSINE-5'-DIPHOSPHATE × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;Solution was made fresh and detergent was added to solve preference orientation issue. cryo-EM vitrification conditions:Cryogen ETHANE;Blot 3S, blot forth 3 Resolution 3.00 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATAD2_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 38–1416; UniProt 1–1379 Author chain B; PDBConstruct 38–1416; UniProt 1–1379 Author chain C; PDBConstruct 38–1416; UniProt 1–1379 Author chain D; PDBConstruct 38–1416; UniProt 1–1379 Author chain E; PDBConstruct 38–1416; UniProt 1–1379 Author chain F; PDBConstruct 38–1416; UniProt 1–1379

Histone H3

OrganismNot specified

UniProt P61830

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain G; UniProt 1–25 Not recorded ATPase histone chaperone YTA7 × 6 (P40340) ADP ADENOSINE-5'-DIPHOSPHATE × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;Solution was made fresh and detergent was added to solve preference orientation issue. cryo-EM vitrification conditions:Cryogen ETHANE;Blot 3S, blot forth 3 Resolution 3.00 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.

37 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H3_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–25; UniProt 1–25

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 7uqj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7uqj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7uqj
Deposition date deposition_date2022-04-19
Structure title titleCryo-EM structure of the S. cerevisiae chromatin remodeler Yta7 hexamer bound to ATPgS and histone H3 tail in state II
Keywords keywordsAAA+ ATPase, chromatin remodeler, TRANSFERASE; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.38
Radius of gyration Rg (electron density) rg_electron47.05
Forward intensity I(0) i02128450000.00
Molecular weight molecular_weight397810.0 kDa
Excluded volume excluded_volume503570 ų
Envelope volume envelope_volume675100 ų
Hydration-shell volume shell_volume111680 ų
Envelope diameter envelope_diameter153.4
Shell Rg shell_rg56.96
Envelope Rg envelope_rg46.53
Shape Rg shape_rg47.05
Total Rg total_rg47.38
Total atoms total_atoms27983
Residues n_residues3495
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 dmax148.5
Rg (real space) rg_real47.05
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real2.1280e+09
I(0) uncertainty (real space) i0_real_error3.5720e+07
Rg (reciprocal space) rg_reciprocal47.38
I(0) (reciprocal space) i0_reciprocal2129000000.0000
Solution quality estimate total_estimate0.6593
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.5
Skewness Skewness skewness0.128
Kurtosis Kurtosis kurtosis-0.492
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha362100000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.899; Stabil: 1.000; Sysdev: 0.006; Positv: 1.000; Valcen: 0.956; Smooth: 0.896

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)