7nyz

Cryo-EM structure of the MukBEF-MatP-DNA monomer (partially open conformation)

Method: ELECTRON MICROSCOPY Dmax: 260.6 Å Quality: GOOD

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 × 10 DNA 4 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain A; UniProt 1–1482 Chain B; UniProt 1–1482 Mutation:E1407Q Chromosome partition protein MukF × 2 (A0A0F7LMQ4) Chromosome partition protein MukE × 2 (A0A0F7LPV6) Acyl carrier protein × 2 (A0A6D2XA84) Macrodomain Ter protein × 2 (A0A0F7LUV5) matS2 DNA 80 b, oligo FBA769 × 1 matS2 DNA 80 b, oligo FBA770 × 1 DNA 80 b × 2 MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 PNS 4'-PHOSPHOPANTETHEINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.50 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 A; PDBConstruct 1–1482; UniProt 1–1482 Author chain B; 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 × 10 DNA 4 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain C; UniProt 1–440 Chain D; UniProt 1–440 Not recorded Chromosome partition protein MukB × 2 (A0A0F7LRY2) Chromosome partition protein MukE × 2 (A0A0F7LPV6) Acyl carrier protein × 2 (A0A6D2XA84) Macrodomain Ter protein × 2 (A0A0F7LUV5) matS2 DNA 80 b, oligo FBA769 × 1 matS2 DNA 80 b, oligo FBA770 × 1 DNA 80 b × 2 MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 PNS 4'-PHOSPHOPANTETHEINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.50 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 C; PDBConstruct 1–440; UniProt 1–440 Author chain D; 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 × 10 DNA 4 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain E; UniProt 1–240 Chain F; UniProt 1–240 Not recorded Chromosome partition protein MukB × 2 (A0A0F7LRY2) Chromosome partition protein MukF × 2 (A0A0F7LMQ4) Acyl carrier protein × 2 (A0A6D2XA84) Macrodomain Ter protein × 2 (A0A0F7LUV5) matS2 DNA 80 b, oligo FBA769 × 1 matS2 DNA 80 b, oligo FBA770 × 1 DNA 80 b × 2 MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 PNS 4'-PHOSPHOPANTETHEINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.50 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 E; PDBConstruct 1–240; UniProt 1–240 Author chain F; 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 × 10 DNA 4 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain G; UniProt 1–78 Chain H; UniProt 1–78 Not recorded Chromosome partition protein MukB × 2 (A0A0F7LRY2) Chromosome partition protein MukF × 2 (A0A0F7LMQ4) Chromosome partition protein MukE × 2 (A0A0F7LPV6) Macrodomain Ter protein × 2 (A0A0F7LUV5) matS2 DNA 80 b, oligo FBA769 × 1 matS2 DNA 80 b, oligo FBA770 × 1 DNA 80 b × 2 MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 PNS 4'-PHOSPHOPANTETHEINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.50 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 G; PDBConstruct 1–78; UniProt 1–78 Author chain H; 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 × 10 DNA 4 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain I; UniProt 1–151 Chain J; UniProt 1–151 Not recorded Chromosome partition protein MukB × 2 (A0A0F7LRY2) Chromosome partition protein MukF × 2 (A0A0F7LMQ4) Chromosome partition protein MukE × 2 (A0A0F7LPV6) Acyl carrier protein × 2 (A0A6D2XA84) matS2 DNA 80 b, oligo FBA769 × 1 matS2 DNA 80 b, oligo FBA770 × 1 DNA 80 b × 2 MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 PNS 4'-PHOSPHOPANTETHEINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.50 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 I; PDBConstruct 1–151; UniProt 1–151 Author chain J; 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 7nyz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7nyz
Deposition date deposition_date2021-03-23
Structure title titleCryo-EM structure of the MukBEF-MatP-DNA monomer (partially open conformation)
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_guinier88.45
Radius of gyration Rg (electron density) rg_electron91.79
Forward intensity I(0) i04320890000.00
Molecular weight molecular_weight515270.0 kDa
Excluded volume excluded_volume628960 ų
Envelope volume envelope_volume1141600 ų
Hydration-shell volume shell_volume123140 ų
Envelope diameter envelope_diameter337.8
Shell Rg shell_rg66.28
Envelope Rg envelope_rg91.07
Shape Rg shape_rg91.91
Total Rg total_rg91.04
Total atoms total_atoms70851
Residues n_residues4290
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 dmax260.6
Rg (real space) rg_real83.08
Rg uncertainty (real space) rg_real_error1.83
I(0) (real space) i0_real4.1690e+09
I(0) uncertainty (real space) i0_real_error9.8010e+07
Rg (reciprocal space) rg_reciprocal80.42
I(0) (reciprocal space) i0_reciprocal4222000000.0000
Solution quality estimate total_estimate0.8866
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary72.4
Skewness Skewness skewness0.661
Kurtosis Kurtosis kurtosis-0.276
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha0.3793
Highest regularization parameter α highest_alpha135700000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.793; Stabil: 0.973; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.235

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (2)

9. Files and Curves (10)