7nyw

Cryo-EM structure of the MukBEF-MatP-DNA head module

Method: ELECTRON MICROSCOPY Dmax: 192.4 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 3.10 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.

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 3.10 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.

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 3.10 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.

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 3.10 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 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 3.10 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.

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 7nyw

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7nyw
Deposition date deposition_date2021-03-23
Structure title titleCryo-EM structure of the MukBEF-MatP-DNA head module
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_guinier55.81
Radius of gyration Rg (electron density) rg_electron56.03
Forward intensity I(0) i02092870000.00
Molecular weight molecular_weight354520.0 kDa
Excluded volume excluded_volume432270 ų
Envelope volume envelope_volume674880 ų
Hydration-shell volume shell_volume99954 ų
Envelope diameter envelope_diameter200.0
Shell Rg shell_rg59.52
Envelope Rg envelope_rg54.89
Shape Rg shape_rg56.05
Total Rg total_rg56.07
Total atoms total_atoms48634
Residues n_residues2899
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 dmax192.4
Rg (real space) rg_real55.84
Rg uncertainty (real space) rg_real_error1.97
I(0) (real space) i0_real2.0930e+09
I(0) uncertainty (real space) i0_real_error4.4120e+07
Rg (reciprocal space) rg_reciprocal55.76
I(0) (reciprocal space) i0_reciprocal2093000000.0000
Solution quality estimate total_estimate0.8746
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.8
Skewness Skewness skewness0.323
Kurtosis Kurtosis kurtosis-0.440
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha309200000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.807

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id7nywE01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily2250
Domain ID domain_id7nywE02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily2260 — MukE-like family, C-terminal domain
Domain ID domain_id7nywF01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily2250
Domain ID domain_id7nywF02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily2260 — MukE-like family, C-terminal domain
Domain ID domain_id7nywI01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily380 — MatP, N-terminal domain
Domain ID domain_id7nywI02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1220 — Arc Repressor Mutant
Homologous superfamily homologous superfamily10 — Met repressor-like
Domain ID domain_id7nywJ01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1270 — Substrate Binding Domain Of Dnak; Chain:A; Domain 2
Homologous superfamily homologous superfamily380 — MatP, N-terminal domain
Domain ID domain_id7nywJ02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1220 — Arc Repressor Mutant
Homologous superfamily homologous superfamily10 — Met repressor-like

8. Citations (2)

9. Files and Curves (10)