7nz3

Cryo-EM structure of apposed MukBEF-MatP monomers on DNA

Method: ELECTRON MICROSCOPY Dmax: 279.1 Å Quality: EXCELLENT

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

Chromosome partition protein MukB

Photorhabdus thracensis

UniProt A0A0F7LRY2

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 × 20 DNA 4 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain A1; UniProt 1–1482 Chain A2; UniProt 1–1482 Chain B1; UniProt 1–1482 Chain B2; UniProt 1–1482 Mutation:E1407Q Chromosome partition protein MukF × 4 (A0A0F7LMQ4) Chromosome partition protein MukE × 4 (A0A0F7LPV6) Acyl carrier protein × 4 (A0A6D2XA84) Macrodomain Ter protein × 4 (A0A0F7LUV5) matS2 DNA 80 b, oligo FBA769 × 2 matS2 DNA 80 b, oligo FBA770 × 2 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 PNS 4'-PHOSPHOPANTETHEINE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 11.00 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0F7LRY2_9GAMM
Isoform
PDB entities 1
Chains and sequence ranges Author chain A1; PDBConstruct 1–1482; UniProt 1–1482 Author chain A2; PDBConstruct 1–1482; UniProt 1–1482 Author chain B1; PDBConstruct 1–1482; UniProt 1–1482 Author chain B2; PDBConstruct 1–1482; UniProt 1–1482

Chromosome partition protein MukF

Photorhabdus thracensis

UniProt A0A0F7LMQ4

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 × 20 DNA 4 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain C1; UniProt 1–440 Chain C2; UniProt 1–440 Chain D1; UniProt 1–440 Chain D2; UniProt 1–440 Not recorded Chromosome partition protein MukB × 4 (A0A0F7LRY2) Chromosome partition protein MukE × 4 (A0A0F7LPV6) Acyl carrier protein × 4 (A0A6D2XA84) Macrodomain Ter protein × 4 (A0A0F7LUV5) matS2 DNA 80 b, oligo FBA769 × 2 matS2 DNA 80 b, oligo FBA770 × 2 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 PNS 4'-PHOSPHOPANTETHEINE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 11.00 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0F7LMQ4_9GAMM
Isoform
PDB entities 2
Chains and sequence ranges Author chain C1; PDBConstruct 1–440; UniProt 1–440 Author chain C2; PDBConstruct 1–440; UniProt 1–440 Author chain D1; PDBConstruct 1–440; UniProt 1–440 Author chain D2; PDBConstruct 1–440; UniProt 1–440

Chromosome partition protein MukE

Photorhabdus thracensis

UniProt A0A0F7LPV6

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 × 20 DNA 4 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain E1; UniProt 1–240 Chain E2; UniProt 1–240 Chain F1; UniProt 1–240 Chain F2; UniProt 1–240 Not recorded Chromosome partition protein MukB × 4 (A0A0F7LRY2) Chromosome partition protein MukF × 4 (A0A0F7LMQ4) Acyl carrier protein × 4 (A0A6D2XA84) Macrodomain Ter protein × 4 (A0A0F7LUV5) matS2 DNA 80 b, oligo FBA769 × 2 matS2 DNA 80 b, oligo FBA770 × 2 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 PNS 4'-PHOSPHOPANTETHEINE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 11.00 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0F7LPV6_9GAMM
Isoform
PDB entities 3
Chains and sequence ranges Author chain E1; PDBConstruct 1–240; UniProt 1–240 Author chain E2; PDBConstruct 1–240; UniProt 1–240 Author chain F1; PDBConstruct 1–240; UniProt 1–240 Author chain F2; PDBConstruct 1–240; UniProt 1–240

Acyl carrier protein

OrganismNot specified

UniProt A0A6D2XA84

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 × 20 DNA 4 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain G1; UniProt 1–78 Chain G2; UniProt 1–78 Chain H1; UniProt 1–78 Chain H2; UniProt 1–78 Not recorded Chromosome partition protein MukB × 4 (A0A0F7LRY2) Chromosome partition protein MukF × 4 (A0A0F7LMQ4) Chromosome partition protein MukE × 4 (A0A0F7LPV6) Macrodomain Ter protein × 4 (A0A0F7LUV5) matS2 DNA 80 b, oligo FBA769 × 2 matS2 DNA 80 b, oligo FBA770 × 2 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 PNS 4'-PHOSPHOPANTETHEINE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 11.00 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.

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

View Construct and Data Evidence
UniProt name A0A6D2XA84_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain G1; PDBConstruct 1–78; UniProt 1–78 Author chain G2; PDBConstruct 1–78; UniProt 1–78 Author chain H1; PDBConstruct 1–78; UniProt 1–78 Author chain H2; PDBConstruct 1–78; UniProt 1–78

Macrodomain Ter protein

Photorhabdus thracensis

UniProt A0A0F7LUV5

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 × 20 DNA 4 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain I1; UniProt 1–151 Chain I2; UniProt 1–151 Chain J1; UniProt 1–151 Chain J2; UniProt 1–151 Not recorded Chromosome partition protein MukB × 4 (A0A0F7LRY2) Chromosome partition protein MukF × 4 (A0A0F7LMQ4) Chromosome partition protein MukE × 4 (A0A0F7LPV6) Acyl carrier protein × 4 (A0A6D2XA84) matS2 DNA 80 b, oligo FBA769 × 2 matS2 DNA 80 b, oligo FBA770 × 2 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 PNS 4'-PHOSPHOPANTETHEINE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 11.00 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.

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

View Construct and Data Evidence
UniProt name A0A0F7LUV5_9GAMM
Isoform
PDB entities 5
Chains and sequence ranges Author chain I1; PDBConstruct 1–151; UniProt 1–151 Author chain I2; PDBConstruct 1–151; UniProt 1–151 Author chain J1; PDBConstruct 1–151; UniProt 1–151 Author chain J2; PDBConstruct 1–151; UniProt 1–151

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 7nz3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7nz3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7nz3
Deposition date deposition_date2021-03-23
Structure title titleCryo-EM structure of apposed MukBEF-MatP monomers on DNA
Keywords keywordsSMC-kleisin complex, ATPase, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron104.50
Forward intensity I(0) i018781300000.00
Molecular weight molecular_weight1062900.0 kDa
Excluded volume excluded_volume1288400 ų
Envelope volume envelope_volume2457800 ų
Hydration-shell volume shell_volume219460 ų
Envelope diameter envelope_diameter461.4
Shell Rg shell_rg88.24
Envelope Rg envelope_rg103.40
Shape Rg shape_rg104.50
Total Rg total_rg104.20
Total atoms total_atoms144972
Residues n_residues8684
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 dmax279.1
Rg (real space) rg_real97.71
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real1.7900e+10
I(0) uncertainty (real space) i0_real_error4.1890e+08
Rg (reciprocal space) rg_reciprocal97.69
I(0) (reciprocal space) i0_reciprocal18420000000.0000
Solution quality estimate total_estimate0.9167
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary111.6
Skewness Skewness skewness0.367
Kurtosis Kurtosis kurtosis-0.473
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.9339
Highest regularization parameter α highest_alpha581500000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.011; Oscil: 0.991; Stabil: 0.976; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.039

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (2)

9. Files and Curves (10)