5tj5

Atomic model for the membrane-embedded motor of a eukaryotic V-ATPase

Method: ELECTRON MICROSCOPY Dmax: 130.3 Å Quality: GOOD

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

V-type proton ATPase subunit a

OrganismNot specified

UniProt P32563

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain A; UniProt 400–829 Not recorded ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit f × 1 V-type proton ATPase subunit d × 1 (P32366) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM Tris-HCl pH 7.5, 150 mM NaCl, 10 micro M Bafilomycin cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;Modified for ethane/propane Resolution 3.90 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.

31 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPH1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 251–680; UniProt 400–829

;V-type proton ATPase subunit c'' ;

OrganismNot specified

UniProt P23968

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain B; UniProt 1–213 Not recorded V-type proton ATPase subunit a × 1 (P32563) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit f × 1 V-type proton ATPase subunit d × 1 (P32366) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM Tris-HCl pH 7.5, 150 mM NaCl, 10 micro M Bafilomycin cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;Modified for ethane/propane Resolution 3.90 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.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATO_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–213; UniProt 1–213

;V-type proton ATPase subunit c' ;

OrganismNot specified

UniProt P32842

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain D; UniProt 17–163 Not recorded V-type proton ATPase subunit a × 1 (P32563) ;V-type proton ATPase subunit c'' ; × 1 (P23968) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit f × 1 V-type proton ATPase subunit d × 1 (P32366) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM Tris-HCl pH 7.5, 150 mM NaCl, 10 micro M Bafilomycin cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;Modified for ethane/propane Resolution 3.90 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.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATL2_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–147; UniProt 17–163

V-type proton ATPase subunit c

OrganismNot specified

UniProt P25515

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain E; UniProt 9–158 Chain F; UniProt 9–158 Chain G; UniProt 9–158 Chain H; UniProt 9–158 Chain I; UniProt 9–158 Chain J; UniProt 9–158 Chain M; UniProt 9–158 Chain N; UniProt 9–158 Not recorded V-type proton ATPase subunit a × 1 (P32563) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit f × 1 V-type proton ATPase subunit d × 1 (P32366) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM Tris-HCl pH 7.5, 150 mM NaCl, 10 micro M Bafilomycin cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;Modified for ethane/propane Resolution 3.90 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.

32 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VATL1_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–150; UniProt 9–158 Author chain F; PDBConstruct 1–150; UniProt 9–158 Author chain G; PDBConstruct 1–150; UniProt 9–158 Author chain H; PDBConstruct 1–150; UniProt 9–158 Author chain I; PDBConstruct 1–150; UniProt 9–158 Author chain J; PDBConstruct 1–150; UniProt 9–158 Author chain M; PDBConstruct 1–150; UniProt 9–158 Author chain N; PDBConstruct 1–150; UniProt 9–158

V-type proton ATPase subunit e

OrganismNot specified

UniProt Q3E7B6

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain L; UniProt 5–61 Not recorded V-type proton ATPase subunit a × 1 (P32563) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit f × 1 V-type proton ATPase subunit d × 1 (P32366) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM Tris-HCl pH 7.5, 150 mM NaCl, 10 micro M Bafilomycin cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;Modified for ethane/propane Resolution 3.90 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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VA0E_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain L; PDBConstruct 1–57; UniProt 5–61

V-type proton ATPase subunit d

OrganismNot specified

UniProt P32366

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain P; UniProt 176–201 Chain P; UniProt 284–341 Chain P; UniProt 4–155 Not recorded V-type proton ATPase subunit a × 1 (P32563) ;V-type proton ATPase subunit c'' ; × 1 (P23968) ;V-type proton ATPase subunit c' ; × 1 (P32842) V-type proton ATPase subunit c × 8 (P25515) V-type proton ATPase subunit e × 1 (Q3E7B6) V-type proton ATPase subunit f × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM Tris-HCl pH 7.5, 150 mM NaCl, 10 micro M Bafilomycin cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;Modified for ethane/propane Resolution 3.90 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.

32 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VA0D_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain P; PDBConstruct 173–198; UniProt 176–201 Author chain P; PDBConstruct 240–297; UniProt 284–341 Author chain P; PDBConstruct 1–152; UniProt 4–155

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 5tj5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5tj5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5tj5
Deposition date deposition_date2016-10-03
Structure title titleAtomic model for the membrane-embedded motor of a eukaryotic V-ATPase
Keywords keywordsRotary ATPase, Vacuolar-type ATPase, Electron Cryomicroscopy, Vo region, Membrane protein, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.03
Radius of gyration Rg (electron density) rg_electron40.81
Forward intensity I(0) i0677604000.00
Molecular weight molecular_weight210590.0 kDa
Excluded volume excluded_volume261610 ų
Envelope volume envelope_volume422090 ų
Hydration-shell volume shell_volume82743 ų
Envelope diameter envelope_diameter137.5
Shell Rg shell_rg49.12
Envelope Rg envelope_rg39.92
Shape Rg shape_rg40.87
Total Rg total_rg41.07
Total atoms total_atoms14976
Residues n_residues2467
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 dmax130.3
Rg (real space) rg_real41.79
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real6.7760e+08
I(0) uncertainty (real space) i0_real_error1.1370e+07
Rg (reciprocal space) rg_reciprocal42.03
I(0) (reciprocal space) i0_reciprocal677800000.0000
Solution quality estimate total_estimate0.8862
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.9
Skewness Skewness skewness0.106
Kurtosis Kurtosis kurtosis-0.423
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha72120000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.905

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id5tj5E00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily610 — lithium bound rotor ring of v- atpase

8. Citations (1)

9. Files and Curves (10)