9es8

Cryo-EM structure of Spinacia oleracea cytochrome b6f with decylplastoquinone bound at plastoquionol reduction site

Method: ELECTRON MICROSCOPY Dmax: 142.7 Å Quality: GOOD

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

Cytochrome b6

OrganismNot specified

UniProt P00165

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain A; UniProt 1–215 Chain I; UniProt 1–215 Not recorded Cytochrome b6-f complex subunit 4 × 2 (P00166) Cytochrome f × 2 (P16013) Cytochrome b6-f complex iron-sulfur subunit, chloroplastic × 2 (P08980) Cytochrome b6-f complex subunit 6 × 2 (Q9M3L0) Cytochrome b6-f complex subunit 7 × 2 (A0A9R0IV89) Cytochrome b6-f complex subunit 5 × 2 (P69461) Cytochrome b6-f complex subunit 8 × 2 (P61045) Thylakoid soluble phosphoprotein × 2 (Q8GT36) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 A1H65 Decylplastoquinone × 2 LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE × 2 CLA CHLOROPHYLL A × 2 UMQ UNDECYL-MALTOSIDE × 4 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 BCR BETA-CAROTENE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;final concentration of plastocyanin was 0.34 mM cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.24 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYB6_SPIOL
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–215; UniProt 1–215 Author chain I; PDBConstruct 1–215; UniProt 1–215

Cytochrome b6-f complex subunit 4

OrganismNot specified

UniProt P00166

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain B; UniProt 1–160 Chain J; UniProt 1–160 Not recorded Cytochrome b6 × 2 (P00165) Cytochrome f × 2 (P16013) Cytochrome b6-f complex iron-sulfur subunit, chloroplastic × 2 (P08980) Cytochrome b6-f complex subunit 6 × 2 (Q9M3L0) Cytochrome b6-f complex subunit 7 × 2 (A0A9R0IV89) Cytochrome b6-f complex subunit 5 × 2 (P69461) Cytochrome b6-f complex subunit 8 × 2 (P61045) Thylakoid soluble phosphoprotein × 2 (Q8GT36) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 A1H65 Decylplastoquinone × 2 LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE × 2 CLA CHLOROPHYLL A × 2 UMQ UNDECYL-MALTOSIDE × 4 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 BCR BETA-CAROTENE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;final concentration of plastocyanin was 0.34 mM cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.24 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PETD_SPIOL
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–160; UniProt 1–160 Author chain J; PDBConstruct 1–160; UniProt 1–160

Cytochrome f

OrganismNot specified

UniProt P16013

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain C; UniProt 1–320 Chain K; UniProt 1–320 Not recorded Cytochrome b6 × 2 (P00165) Cytochrome b6-f complex subunit 4 × 2 (P00166) Cytochrome b6-f complex iron-sulfur subunit, chloroplastic × 2 (P08980) Cytochrome b6-f complex subunit 6 × 2 (Q9M3L0) Cytochrome b6-f complex subunit 7 × 2 (A0A9R0IV89) Cytochrome b6-f complex subunit 5 × 2 (P69461) Cytochrome b6-f complex subunit 8 × 2 (P61045) Thylakoid soluble phosphoprotein × 2 (Q8GT36) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 A1H65 Decylplastoquinone × 2 LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE × 2 CLA CHLOROPHYLL A × 2 UMQ UNDECYL-MALTOSIDE × 4 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 BCR BETA-CAROTENE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;final concentration of plastocyanin was 0.34 mM cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.24 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYF_SPIOL
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–320; UniProt 1–320 Author chain K; PDBConstruct 1–320; UniProt 1–320

Cytochrome b6-f complex iron-sulfur subunit, chloroplastic

OrganismNot specified

UniProt P08980

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain D; UniProt 1–230 Chain L; UniProt 1–230 Not recorded Cytochrome b6 × 2 (P00165) Cytochrome b6-f complex subunit 4 × 2 (P00166) Cytochrome f × 2 (P16013) Cytochrome b6-f complex subunit 6 × 2 (Q9M3L0) Cytochrome b6-f complex subunit 7 × 2 (A0A9R0IV89) Cytochrome b6-f complex subunit 5 × 2 (P69461) Cytochrome b6-f complex subunit 8 × 2 (P61045) Thylakoid soluble phosphoprotein × 2 (Q8GT36) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 A1H65 Decylplastoquinone × 2 LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE × 2 CLA CHLOROPHYLL A × 2 UMQ UNDECYL-MALTOSIDE × 4 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 BCR BETA-CAROTENE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;final concentration of plastocyanin was 0.34 mM cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.24 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 UCRIA_SPIOL
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–230; UniProt 1–230 Author chain L; PDBConstruct 1–230; UniProt 1–230

Cytochrome b6-f complex subunit 6

OrganismNot specified

UniProt Q9M3L0

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain E; UniProt 1–31 Chain M; UniProt 1–31 Not recorded Cytochrome b6 × 2 (P00165) Cytochrome b6-f complex subunit 4 × 2 (P00166) Cytochrome f × 2 (P16013) Cytochrome b6-f complex iron-sulfur subunit, chloroplastic × 2 (P08980) Cytochrome b6-f complex subunit 7 × 2 (A0A9R0IV89) Cytochrome b6-f complex subunit 5 × 2 (P69461) Cytochrome b6-f complex subunit 8 × 2 (P61045) Thylakoid soluble phosphoprotein × 2 (Q8GT36) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 A1H65 Decylplastoquinone × 2 LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE × 2 CLA CHLOROPHYLL A × 2 UMQ UNDECYL-MALTOSIDE × 4 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 BCR BETA-CAROTENE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;final concentration of plastocyanin was 0.34 mM cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.24 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PETL_SPIOL
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–31; UniProt 1–31 Author chain M; PDBConstruct 1–31; UniProt 1–31

Cytochrome b6-f complex subunit 7

OrganismNot specified

UniProt A0A9R0IV89

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain F; UniProt 1–131 Chain N; UniProt 1–131 Not recorded Cytochrome b6 × 2 (P00165) Cytochrome b6-f complex subunit 4 × 2 (P00166) Cytochrome f × 2 (P16013) Cytochrome b6-f complex iron-sulfur subunit, chloroplastic × 2 (P08980) Cytochrome b6-f complex subunit 6 × 2 (Q9M3L0) Cytochrome b6-f complex subunit 5 × 2 (P69461) Cytochrome b6-f complex subunit 8 × 2 (P61045) Thylakoid soluble phosphoprotein × 2 (Q8GT36) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 A1H65 Decylplastoquinone × 2 LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE × 2 CLA CHLOROPHYLL A × 2 UMQ UNDECYL-MALTOSIDE × 4 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 BCR BETA-CAROTENE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;final concentration of plastocyanin was 0.34 mM cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.24 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A9R0IV89_SPIOL
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–131; UniProt 1–131 Author chain N; PDBConstruct 1–131; UniProt 1–131

Cytochrome b6-f complex subunit 5

OrganismNot specified

UniProt P69461

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain G; UniProt 1–37 Chain O; UniProt 1–37 Not recorded Cytochrome b6 × 2 (P00165) Cytochrome b6-f complex subunit 4 × 2 (P00166) Cytochrome f × 2 (P16013) Cytochrome b6-f complex iron-sulfur subunit, chloroplastic × 2 (P08980) Cytochrome b6-f complex subunit 6 × 2 (Q9M3L0) Cytochrome b6-f complex subunit 7 × 2 (A0A9R0IV89) Cytochrome b6-f complex subunit 8 × 2 (P61045) Thylakoid soluble phosphoprotein × 2 (Q8GT36) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 A1H65 Decylplastoquinone × 2 LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE × 2 CLA CHLOROPHYLL A × 2 UMQ UNDECYL-MALTOSIDE × 4 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 BCR BETA-CAROTENE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;final concentration of plastocyanin was 0.34 mM cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.24 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PETG_SPIOL
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–37; UniProt 1–37 Author chain O; PDBConstruct 1–37; UniProt 1–37

Cytochrome b6-f complex subunit 8

OrganismNot specified

UniProt P61045

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain H; UniProt 1–29 Chain P; UniProt 1–29 Not recorded Cytochrome b6 × 2 (P00165) Cytochrome b6-f complex subunit 4 × 2 (P00166) Cytochrome f × 2 (P16013) Cytochrome b6-f complex iron-sulfur subunit, chloroplastic × 2 (P08980) Cytochrome b6-f complex subunit 6 × 2 (Q9M3L0) Cytochrome b6-f complex subunit 7 × 2 (A0A9R0IV89) Cytochrome b6-f complex subunit 5 × 2 (P69461) Thylakoid soluble phosphoprotein × 2 (Q8GT36) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 A1H65 Decylplastoquinone × 2 LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE × 2 CLA CHLOROPHYLL A × 2 UMQ UNDECYL-MALTOSIDE × 4 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 BCR BETA-CAROTENE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;final concentration of plastocyanin was 0.34 mM cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.24 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PETN_SPIOL
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–29; UniProt 1–29 Author chain P; PDBConstruct 1–29; UniProt 1–29

Thylakoid soluble phosphoprotein

OrganismNot specified

UniProt Q8GT36

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain Q; UniProt 1–103 Chain R; UniProt 1–103 Not recorded Cytochrome b6 × 2 (P00165) Cytochrome b6-f complex subunit 4 × 2 (P00166) Cytochrome f × 2 (P16013) Cytochrome b6-f complex iron-sulfur subunit, chloroplastic × 2 (P08980) Cytochrome b6-f complex subunit 6 × 2 (Q9M3L0) Cytochrome b6-f complex subunit 7 × 2 (A0A9R0IV89) Cytochrome b6-f complex subunit 5 × 2 (P69461) Cytochrome b6-f complex subunit 8 × 2 (P61045) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 4 A1H65 Decylplastoquinone × 2 LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE × 2 CLA CHLOROPHYLL A × 2 UMQ UNDECYL-MALTOSIDE × 4 SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 BCR BETA-CAROTENE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;final concentration of plastocyanin was 0.34 mM cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.24 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8GT36_SPIOL
Isoform
PDB entities 9
Chains and sequence ranges Author chain Q; PDBConstruct 1–103; UniProt 1–103 Author chain R; PDBConstruct 1–103; UniProt 1–103

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 9es8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9es8
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9es8
Deposition date deposition_date2024-03-25
Structure title titleCryo-EM structure of Spinacia oleracea cytochrome b6f with decylplastoquinone bound at plastoquionol reduction site
Keywords keywords;b6f complex, photosynthesis, membrane protein, electron transport, proton transport, quinone catalysis, water channels, OXIDOREDUCTASE ;; OXIDOREDUCTASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.44
Radius of gyration Rg (electron density) rg_electron43.27
Forward intensity I(0) i0616402000.00
Molecular weight molecular_weight228190.0 kDa
Excluded volume excluded_volume295200 ų
Envelope volume envelope_volume407630 ų
Hydration-shell volume shell_volume76952 ų
Envelope diameter envelope_diameter147.7
Shell Rg shell_rg49.71
Envelope Rg envelope_rg42.88
Shape Rg shape_rg43.26
Total Rg total_rg43.66
Total atoms total_atoms16090
Residues n_residues1948
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 dmax142.7
Rg (real space) rg_real44.28
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real6.1640e+08
I(0) uncertainty (real space) i0_real_error1.1710e+07
Rg (reciprocal space) rg_reciprocal44.44
I(0) (reciprocal space) i0_reciprocal616500000.0000
Solution quality estimate total_estimate0.8285
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.5
Skewness Skewness skewness0.183
Kurtosis Kurtosis kurtosis-0.493
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha66760000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.924; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (19)

8. Citations (1)

9. Files and Curves (10)