6b2z

Cryo-EM structure of the dimeric FO region of yeast mitochondrial ATP synthase

Method: ELECTRON MICROSCOPY Dmax: 187.4 Å Quality: GOOD

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

ATP synthase subunit c, mitochondrial

OrganismNot specified

UniProt P61829

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 × 38 PDB declaration: 38-meric(38) Consistent with protein copy count Chain 0; UniProt 1–76 Chain 1; UniProt 1–76 Chain 2; UniProt 1–76 Chain 3; UniProt 1–76 Chain 4; UniProt 1–76 Chain 5; UniProt 1–76 Chain 6; UniProt 1–76 Chain 7; UniProt 1–76 Chain 8; UniProt 1–76 Chain 9; UniProt 1–76 Chain B; UniProt 1–76 Chain C; UniProt 1–76 Chain D; UniProt 1–76 Chain E; UniProt 1–76 Chain F; UniProt 1–76 Chain G; UniProt 1–76 Chain H; UniProt 1–76 Chain I; UniProt 1–76 Chain J; UniProt 1–76 Chain K; UniProt 1–76 Not recorded ATP synthase protein 8 × 2 (P00856) ATP synthase subunit a × 2 (P00854) ATP synthase subunit b × 2 (P05626) ATP synthase subunit d, mitochondrial × 2 (P30902) ATP synthase subunit e, mitochondrial × 2 ATP synthase subunit f, mitochondrial × 2 (Q06405) ATP synthase subunit g × 2 ATP synthase subunit j, mitochondrial × 2 (P81450) ATP synthase subunit k, mitochondrial × 2 (P81451) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;blot for 26 seconds before plunging Resolution 3.60 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.

48 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP9_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain 0; PDBConstruct 1–76; UniProt 1–76 Author chain 1; PDBConstruct 1–76; UniProt 1–76 Author chain 2; PDBConstruct 1–76; UniProt 1–76 Author chain 3; PDBConstruct 1–76; UniProt 1–76 Author chain 4; PDBConstruct 1–76; UniProt 1–76 Author chain 5; PDBConstruct 1–76; UniProt 1–76 Author chain 6; PDBConstruct 1–76; UniProt 1–76 Author chain 7; PDBConstruct 1–76; UniProt 1–76 Author chain 8; PDBConstruct 1–76; UniProt 1–76 Author chain 9; PDBConstruct 1–76; UniProt 1–76 Author chain B; PDBConstruct 1–76; UniProt 1–76 Author chain C; PDBConstruct 1–76; UniProt 1–76 Author chain D; PDBConstruct 1–76; UniProt 1–76 Author chain E; PDBConstruct 1–76; UniProt 1–76 Author chain F; PDBConstruct 1–76; UniProt 1–76 Author chain G; PDBConstruct 1–76; UniProt 1–76 Author chain H; PDBConstruct 1–76; UniProt 1–76 Author chain I; PDBConstruct 1–76; UniProt 1–76 Author chain J; PDBConstruct 1–76; UniProt 1–76 Author chain K; PDBConstruct 1–76; UniProt 1–76

ATP synthase protein 8

OrganismNot specified

UniProt P00856

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 × 38 PDB declaration: 38-meric(38) Consistent with protein copy count Chain A; UniProt 1–48 Chain L; UniProt 1–48 Not recorded ATP synthase subunit c, mitochondrial × 20 (P61829) ATP synthase subunit a × 2 (P00854) ATP synthase subunit b × 2 (P05626) ATP synthase subunit d, mitochondrial × 2 (P30902) ATP synthase subunit e, mitochondrial × 2 ATP synthase subunit f, mitochondrial × 2 (Q06405) ATP synthase subunit g × 2 ATP synthase subunit j, mitochondrial × 2 (P81450) ATP synthase subunit k, mitochondrial × 2 (P81451) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;blot for 26 seconds before plunging Resolution 3.60 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.

39 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP8_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–48; UniProt 1–48 Author chain L; PDBConstruct 1–48; UniProt 1–48

ATP synthase subunit a

OrganismNot specified

UniProt P00854

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 × 38 PDB declaration: 38-meric(38) Consistent with protein copy count Chain M; UniProt 11–259 Chain a; UniProt 11–259 Not recorded ATP synthase subunit c, mitochondrial × 20 (P61829) ATP synthase protein 8 × 2 (P00856) ATP synthase subunit b × 2 (P05626) ATP synthase subunit d, mitochondrial × 2 (P30902) ATP synthase subunit e, mitochondrial × 2 ATP synthase subunit f, mitochondrial × 2 (Q06405) ATP synthase subunit g × 2 ATP synthase subunit j, mitochondrial × 2 (P81450) ATP synthase subunit k, mitochondrial × 2 (P81451) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;blot for 26 seconds before plunging Resolution 3.60 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.

40 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP6_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain M; PDBConstruct 1–249; UniProt 11–259 Author chain a; PDBConstruct 1–249; UniProt 11–259

ATP synthase subunit b

OrganismNot specified

UniProt P05626

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 × 38 PDB declaration: 38-meric(38) Consistent with protein copy count Chain N; UniProt 36–244 Chain b; UniProt 36–244 Not recorded ATP synthase subunit c, mitochondrial × 20 (P61829) ATP synthase protein 8 × 2 (P00856) ATP synthase subunit a × 2 (P00854) ATP synthase subunit d, mitochondrial × 2 (P30902) ATP synthase subunit e, mitochondrial × 2 ATP synthase subunit f, mitochondrial × 2 (Q06405) ATP synthase subunit g × 2 ATP synthase subunit j, mitochondrial × 2 (P81450) ATP synthase subunit k, mitochondrial × 2 (P81451) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;blot for 26 seconds before plunging Resolution 3.60 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.

40 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPF_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain N; PDBConstruct 1–209; UniProt 36–244 Author chain b; PDBConstruct 1–209; UniProt 36–244

ATP synthase subunit d, mitochondrial

OrganismNot specified

UniProt P30902

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 × 38 PDB declaration: 38-meric(38) Consistent with protein copy count Chain O; UniProt 2–174 Chain d; UniProt 2–174 Not recorded ATP synthase subunit c, mitochondrial × 20 (P61829) ATP synthase protein 8 × 2 (P00856) ATP synthase subunit a × 2 (P00854) ATP synthase subunit b × 2 (P05626) ATP synthase subunit e, mitochondrial × 2 ATP synthase subunit f, mitochondrial × 2 (Q06405) ATP synthase subunit g × 2 ATP synthase subunit j, mitochondrial × 2 (P81450) ATP synthase subunit k, mitochondrial × 2 (P81451) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;blot for 26 seconds before plunging Resolution 3.60 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.

41 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP7_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain O; PDBConstruct 1–173; UniProt 2–174 Author chain d; PDBConstruct 1–173; UniProt 2–174

ATP synthase subunit f, mitochondrial

OrganismNot specified

UniProt Q06405

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 × 38 PDB declaration: 38-meric(38) Consistent with protein copy count Chain Q; UniProt 7–101 Chain f; UniProt 7–101 Not recorded ATP synthase subunit c, mitochondrial × 20 (P61829) ATP synthase protein 8 × 2 (P00856) ATP synthase subunit a × 2 (P00854) ATP synthase subunit b × 2 (P05626) ATP synthase subunit d, mitochondrial × 2 (P30902) ATP synthase subunit e, mitochondrial × 2 ATP synthase subunit g × 2 ATP synthase subunit j, mitochondrial × 2 (P81450) ATP synthase subunit k, mitochondrial × 2 (P81451) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;blot for 26 seconds before plunging Resolution 3.60 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.

41 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATPK_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain Q; PDBConstruct 1–95; UniProt 7–101 Author chain f; PDBConstruct 1–95; UniProt 7–101

ATP synthase subunit j, mitochondrial

OrganismNot specified

UniProt P81450

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 × 38 PDB declaration: 38-meric(38) Consistent with protein copy count Chain S; UniProt 1–59 Chain i; UniProt 1–59 Not recorded ATP synthase subunit c, mitochondrial × 20 (P61829) ATP synthase protein 8 × 2 (P00856) ATP synthase subunit a × 2 (P00854) ATP synthase subunit b × 2 (P05626) ATP synthase subunit d, mitochondrial × 2 (P30902) ATP synthase subunit e, mitochondrial × 2 ATP synthase subunit f, mitochondrial × 2 (Q06405) ATP synthase subunit g × 2 ATP synthase subunit k, mitochondrial × 2 (P81451) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;blot for 26 seconds before plunging Resolution 3.60 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.

39 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATP18_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain S; PDBConstruct 1–59; UniProt 1–59 Author chain i; PDBConstruct 1–59; UniProt 1–59

ATP synthase subunit k, mitochondrial

OrganismNot specified

UniProt P81451

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 × 38 PDB declaration: 38-meric(38) Consistent with protein copy count Chain T; UniProt 1–68 Chain k; UniProt 1–68 Not recorded ATP synthase subunit c, mitochondrial × 20 (P61829) ATP synthase protein 8 × 2 (P00856) ATP synthase subunit a × 2 (P00854) ATP synthase subunit b × 2 (P05626) ATP synthase subunit d, mitochondrial × 2 (P30902) ATP synthase subunit e, mitochondrial × 2 ATP synthase subunit f, mitochondrial × 2 (Q06405) ATP synthase subunit g × 2 ATP synthase subunit j, mitochondrial × 2 (P81450) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;blot for 26 seconds before plunging Resolution 3.60 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 ATP19_YEAST
Isoform
PDB entities 10
Chains and sequence ranges Author chain T; PDBConstruct 1–68; UniProt 1–68 Author chain k; PDBConstruct 1–68; UniProt 1–68

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 6b2z

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6b2z
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6b2z
Deposition date deposition_date2017-09-20
Structure title titleCryo-EM structure of the dimeric FO region of yeast mitochondrial ATP synthase
Keywords keywordsComplex, Dimer, Mitochondrial inner membrane, Proton translocation, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier54.66
Radius of gyration Rg (electron density) rg_electron54.49
Forward intensity I(0) i01062920000.00
Molecular weight molecular_weight303720.0 kDa
Excluded volume excluded_volume392970 ų
Envelope volume envelope_volume596090 ų
Hydration-shell volume shell_volume92548 ų
Envelope diameter envelope_diameter183.4
Shell Rg shell_rg57.22
Envelope Rg envelope_rg51.97
Shape Rg shape_rg54.45
Total Rg total_rg54.74
Total atoms total_atoms21436
Residues n_residues2996
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 dmax187.4
Rg (real space) rg_real54.73
Rg uncertainty (real space) rg_real_error2.11
I(0) (real space) i0_real1.0630e+09
I(0) uncertainty (real space) i0_real_error2.3640e+07
Rg (reciprocal space) rg_reciprocal54.58
I(0) (reciprocal space) i0_reciprocal1063000000.0000
Solution quality estimate total_estimate0.8808
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.2
Skewness Skewness skewness0.306
Kurtosis Kurtosis kurtosis-0.585
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha170500000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.853

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 20 domains

CATH v4.4 (20 domains)

Domain ID domain_id6b2z000
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2z100
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2z200
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2z300
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2z400
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2z500
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2z600
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2z700
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2z800
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2z900
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2zB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2zC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2zD00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2zE00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2zF00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2zG00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2zH00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2zI00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2zJ00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C
Domain ID domain_id6b2zK00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology20 — F1FO ATP Synthase
Homologous superfamily homologous superfamily10 — F1F0 ATP synthase subunit C

8. Citations (1)

9. Files and Curves (10)