7v8l

LolCDE with bound RcsF in nanodiscs

Method: ELECTRON MICROSCOPY Dmax: 135.2 Å Quality: GOOD

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

Lipoprotein-releasing system transmembrane protein LolE

Escherichia coli K-12

UniProt P75958

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 1–414 Not recorded Outer membrane lipoprotein RcsF × 1 (P69411) Lipoprotein-releasing system transmembrane protein LolC × 1 (P0ADC3) Lipoprotein-releasing system ATP-binding protein LolD × 2 (P75957) PCJ (2R)-3-{[(2S)-3-HYDROXY-2-(PALMITOYLAMINO)PROPYL]THIO}PROPANE-1,2-DIYL DIHEXADECANOATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.50 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.

21 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LOLE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 1–414; UniProt 1–414

Outer membrane lipoprotein RcsF

Escherichia coli K-12

UniProt P69411

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 17–134 Not recorded Lipoprotein-releasing system transmembrane protein LolE × 1 (P75958) Lipoprotein-releasing system transmembrane protein LolC × 1 (P0ADC3) Lipoprotein-releasing system ATP-binding protein LolD × 2 (P75957) PCJ (2R)-3-{[(2S)-3-HYDROXY-2-(PALMITOYLAMINO)PROPYL]THIO}PROPANE-1,2-DIYL DIHEXADECANOATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.50 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RCSF_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–118; UniProt 17–134

Lipoprotein-releasing system transmembrane protein LolC

Escherichia coli K-12

UniProt P0ADC3

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–399 Not recorded Lipoprotein-releasing system transmembrane protein LolE × 1 (P75958) Outer membrane lipoprotein RcsF × 1 (P69411) Lipoprotein-releasing system ATP-binding protein LolD × 2 (P75957) PCJ (2R)-3-{[(2S)-3-HYDROXY-2-(PALMITOYLAMINO)PROPYL]THIO}PROPANE-1,2-DIYL DIHEXADECANOATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.50 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.

18 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LOLC_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–399; UniProt 1–399

Lipoprotein-releasing system ATP-binding protein LolD

Escherichia coli K-12

UniProt P75957

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 1–233 Chain F; UniProt 1–233 Not recorded Lipoprotein-releasing system transmembrane protein LolE × 1 (P75958) Outer membrane lipoprotein RcsF × 1 (P69411) Lipoprotein-releasing system transmembrane protein LolC × 1 (P0ADC3) PCJ (2R)-3-{[(2S)-3-HYDROXY-2-(PALMITOYLAMINO)PROPYL]THIO}PROPANE-1,2-DIYL DIHEXADECANOATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.50 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.

21 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LOLD_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–233; UniProt 1–233 Author chain F; PDBConstruct 1–233; UniProt 1–233

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 7v8l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7v8l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7v8l
Deposition date deposition_date2021-08-23
Structure title titleLolCDE with bound RcsF in nanodiscs
Keywords keywordsmembrane protein, ABC transporter, lipoprotein; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.36
Radius of gyration Rg (electron density) rg_electron44.68
Forward intensity I(0) i0257302000.00
Molecular weight molecular_weight135240.0 kDa
Excluded volume excluded_volume171060 ų
Envelope volume envelope_volume249890 ų
Hydration-shell volume shell_volume48642 ų
Envelope diameter envelope_diameter146.8
Shell Rg shell_rg46.42
Envelope Rg envelope_rg44.44
Shape Rg shape_rg44.72
Total Rg total_rg44.61
Total atoms total_atoms9610
Residues n_residues1277
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 dmax135.2
Rg (real space) rg_real45.70
Rg uncertainty (real space) rg_real_error1.26
I(0) (real space) i0_real2.5730e+08
I(0) uncertainty (real space) i0_real_error4.6510e+06
Rg (reciprocal space) rg_reciprocal45.36
I(0) (reciprocal space) i0_reciprocal257200000.0000
Solution quality estimate total_estimate0.7999
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.6
Skewness Skewness skewness0.382
Kurtosis Kurtosis kurtosis-0.823
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29030000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.861; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.815; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)