8twa

Cryo-EM structure of S. cerevisiae Ctf18-RFC-PCNA-PolE-DNA complex

Method: ELECTRON MICROSCOPY Dmax: 192.3 Å Quality: GOOD

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

Chromosome transmission fidelity protein 18

Saccharomyces cerevisiae

UniProt P49956

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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain 1; UniProt 1–741 Chain C; UniProt 715–740 Not recorded Primer DNA × 1 Template DNA × 1 DNA polymerase epsilon catalytic subunit A × 1 (P21951) Chromosome transmission fidelity protein 8 × 1 (P38877) Sister chromatid cohesion protein DCC1 × 1 (P25559) Replication factor C subunit 4 × 1 (P40339) Replication factor C subunit 3 × 1 (P38629) Replication factor C subunit 2 × 1 (P40348) Replication factor C subunit 5 × 1 (P38251) Proliferating cell nuclear antigen × 3 (P15873) SF4 IRON/SULFUR CLUSTER × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTF18_YEAST
Isoform
PDB entities 1, 11
Chains and sequence ranges Author chain C; PDBConstruct 1–26; UniProt 715–740 Author chain 1; PDBConstruct 1–741; UniProt 1–741

DNA polymerase epsilon catalytic subunit A

Saccharomyces cerevisiae

UniProt P21951

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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain E; UniProt 1–2222 Not recorded Chromosome transmission fidelity protein 18 × 1 (P49956) Primer DNA × 1 Template DNA × 1 Chromosome transmission fidelity protein 8 × 1 (P38877) Sister chromatid cohesion protein DCC1 × 1 (P25559) Replication factor C subunit 4 × 1 (P40339) Replication factor C subunit 3 × 1 (P38629) Replication factor C subunit 2 × 1 (P40348) Replication factor C subunit 5 × 1 (P38251) Chromosome transmission fidelity protein 18 × 1 (P49956) Proliferating cell nuclear antigen × 3 (P15873) SF4 IRON/SULFUR CLUSTER × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

33 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOE_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–2222; UniProt 1–2222

Chromosome transmission fidelity protein 8

Saccharomyces cerevisiae

UniProt P38877

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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain D; UniProt 2–133 Not recorded Chromosome transmission fidelity protein 18 × 1 (P49956) Primer DNA × 1 Template DNA × 1 DNA polymerase epsilon catalytic subunit A × 1 (P21951) Sister chromatid cohesion protein DCC1 × 1 (P25559) Replication factor C subunit 4 × 1 (P40339) Replication factor C subunit 3 × 1 (P38629) Replication factor C subunit 2 × 1 (P40348) Replication factor C subunit 5 × 1 (P38251) Chromosome transmission fidelity protein 18 × 1 (P49956) Proliferating cell nuclear antigen × 3 (P15873) SF4 IRON/SULFUR CLUSTER × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTF8_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain D; PDBConstruct 1–132; UniProt 2–133

Sister chromatid cohesion protein DCC1

Saccharomyces cerevisiae

UniProt P25559

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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain B; UniProt 1–380 Not recorded Chromosome transmission fidelity protein 18 × 1 (P49956) Primer DNA × 1 Template DNA × 1 DNA polymerase epsilon catalytic subunit A × 1 (P21951) Chromosome transmission fidelity protein 8 × 1 (P38877) Replication factor C subunit 4 × 1 (P40339) Replication factor C subunit 3 × 1 (P38629) Replication factor C subunit 2 × 1 (P40348) Replication factor C subunit 5 × 1 (P38251) Chromosome transmission fidelity protein 18 × 1 (P49956) Proliferating cell nuclear antigen × 3 (P15873) SF4 IRON/SULFUR CLUSTER × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

8 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DCC1_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain B; PDBConstruct 1–380; UniProt 1–380

Replication factor C subunit 4

Saccharomyces cerevisiae

UniProt P40339

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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain 4; UniProt 4–322 Not recorded Chromosome transmission fidelity protein 18 × 1 (P49956) Primer DNA × 1 Template DNA × 1 DNA polymerase epsilon catalytic subunit A × 1 (P21951) Chromosome transmission fidelity protein 8 × 1 (P38877) Sister chromatid cohesion protein DCC1 × 1 (P25559) Replication factor C subunit 3 × 1 (P38629) Replication factor C subunit 2 × 1 (P40348) Replication factor C subunit 5 × 1 (P38251) Chromosome transmission fidelity protein 18 × 1 (P49956) Proliferating cell nuclear antigen × 3 (P15873) SF4 IRON/SULFUR CLUSTER × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

49 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFC4_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain 4; PDBConstruct 1–319; UniProt 4–322

Replication factor C subunit 3

Saccharomyces cerevisiae

UniProt P38629

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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain 3; UniProt 9–335 Not recorded Chromosome transmission fidelity protein 18 × 1 (P49956) Primer DNA × 1 Template DNA × 1 DNA polymerase epsilon catalytic subunit A × 1 (P21951) Chromosome transmission fidelity protein 8 × 1 (P38877) Sister chromatid cohesion protein DCC1 × 1 (P25559) Replication factor C subunit 4 × 1 (P40339) Replication factor C subunit 2 × 1 (P40348) Replication factor C subunit 5 × 1 (P38251) Chromosome transmission fidelity protein 18 × 1 (P49956) Proliferating cell nuclear antigen × 3 (P15873) SF4 IRON/SULFUR CLUSTER × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

49 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFC3_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain 3; PDBConstruct 1–327; UniProt 9–335

Replication factor C subunit 2

Saccharomyces cerevisiae

UniProt P40348

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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain 2; UniProt 14–353 Not recorded Chromosome transmission fidelity protein 18 × 1 (P49956) Primer DNA × 1 Template DNA × 1 DNA polymerase epsilon catalytic subunit A × 1 (P21951) Chromosome transmission fidelity protein 8 × 1 (P38877) Sister chromatid cohesion protein DCC1 × 1 (P25559) Replication factor C subunit 4 × 1 (P40339) Replication factor C subunit 3 × 1 (P38629) Replication factor C subunit 5 × 1 (P38251) Chromosome transmission fidelity protein 18 × 1 (P49956) Proliferating cell nuclear antigen × 3 (P15873) SF4 IRON/SULFUR CLUSTER × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

49 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFC2_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain 2; PDBConstruct 1–340; UniProt 14–353

Replication factor C subunit 5

Saccharomyces cerevisiae

UniProt P38251

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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain 5; UniProt 4–353 Not recorded Chromosome transmission fidelity protein 18 × 1 (P49956) Primer DNA × 1 Template DNA × 1 DNA polymerase epsilon catalytic subunit A × 1 (P21951) Chromosome transmission fidelity protein 8 × 1 (P38877) Sister chromatid cohesion protein DCC1 × 1 (P25559) Replication factor C subunit 4 × 1 (P40339) Replication factor C subunit 3 × 1 (P38629) Replication factor C subunit 2 × 1 (P40348) Chromosome transmission fidelity protein 18 × 1 (P49956) Proliferating cell nuclear antigen × 3 (P15873) SF4 IRON/SULFUR CLUSTER × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

49 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFC5_YEAST
Isoform
PDB entities 10
Chains and sequence ranges Author chain 5; PDBConstruct 4–353; UniProt 4–353

Proliferating cell nuclear antigen

Saccharomyces cerevisiae

UniProt P15873

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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain X; UniProt 1–258 Chain Y; UniProt 1–258 Chain Z; UniProt 1–258 Not recorded Chromosome transmission fidelity protein 18 × 1 (P49956) Primer DNA × 1 Template DNA × 1 DNA polymerase epsilon catalytic subunit A × 1 (P21951) Chromosome transmission fidelity protein 8 × 1 (P38877) Sister chromatid cohesion protein DCC1 × 1 (P25559) Replication factor C subunit 4 × 1 (P40339) Replication factor C subunit 3 × 1 (P38629) Replication factor C subunit 2 × 1 (P40348) Replication factor C subunit 5 × 1 (P38251) Chromosome transmission fidelity protein 18 × 1 (P49956) SF4 IRON/SULFUR CLUSTER × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

55 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PCNA_YEAST
Isoform
PDB entities 12
Chains and sequence ranges Author chain X; PDBConstruct 1–258; UniProt 1–258 Author chain Y; PDBConstruct 1–258; UniProt 1–258 Author chain Z; PDBConstruct 1–258; UniProt 1–258

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 8twa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8twa
Deposition date deposition_date2023-08-20
Structure title titleCryo-EM structure of S. cerevisiae Ctf18-RFC-PCNA-PolE-DNA complex
Keywords keywordsCtf18, RFC2-5, PCNA, Pol2, DNA, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier58.74
Radius of gyration Rg (electron density) rg_electron58.63
Forward intensity I(0) i02949930000.00
Molecular weight molecular_weight454570.0 kDa
Excluded volume excluded_volume568180 ų
Envelope volume envelope_volume878530 ų
Hydration-shell volume shell_volume124260 ų
Envelope diameter envelope_diameter191.7
Shell Rg shell_rg62.74
Envelope Rg envelope_rg56.13
Shape Rg shape_rg58.64
Total Rg total_rg58.70
Total atoms total_atoms31914
Residues n_residues4024
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 dmax192.3
Rg (real space) rg_real58.70
Rg uncertainty (real space) rg_real_error1.39
I(0) (real space) i0_real2.9500e+09
I(0) uncertainty (real space) i0_real_error5.5410e+07
Rg (reciprocal space) rg_reciprocal58.74
I(0) (reciprocal space) i0_reciprocal2950000000.0000
Solution quality estimate total_estimate0.8675
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.1
Skewness Skewness skewness0.286
Kurtosis Kurtosis kurtosis-0.548
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha260300000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.572

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (16)

8. Citations (1)

9. Files and Curves (10)