6smh

Cryo-electron microscopy structure of a RbcL-Raf1 supercomplex from Synechococcus elongatus PCC 7942

Method: ELECTRON MICROSCOPY Dmax: 155.8 Å Quality: GOOD

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

Ribulose bisphosphate carboxylase large chain

Synechococcus elongatus (strain PCC 7942 / FACHB-805)

UniProt Q31NB3

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain A; UniProt 19–465 Chain B; UniProt 19–465 Chain C; UniProt 19–465 Chain D; UniProt 19–465 Chain E; UniProt 19–465 Chain F; UniProt 19–465 Chain G; UniProt 19–465 Chain H; UniProt 19–465 Not recorded Rubisco accumulation factor 1 (RAF1) peptide × 8 (Q31Q05) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 4.30 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBL_SYNE7
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–447; UniProt 19–465 Author chain B; PDBConstruct 1–447; UniProt 19–465 Author chain C; PDBConstruct 1–447; UniProt 19–465 Author chain D; PDBConstruct 1–447; UniProt 19–465 Author chain E; PDBConstruct 1–447; UniProt 19–465 Author chain F; PDBConstruct 1–447; UniProt 19–465 Author chain G; PDBConstruct 1–447; UniProt 19–465 Author chain H; PDBConstruct 1–447; UniProt 19–465

Rubisco accumulation factor 1 (RAF1) peptide

Synechococcus elongatus (strain PCC 7942 / FACHB-805)

UniProt Q31Q05

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain I; UniProt 13–200 Chain J; UniProt 13–200 Chain K; UniProt 13–200 Chain L; UniProt 13–200 Chain M; UniProt 13–200 Chain N; UniProt 13–200 Chain O; UniProt 13–200 Chain P; UniProt 13–200 Not recorded Ribulose bisphosphate carboxylase large chain × 8 (Q31NB3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 4.30 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q31Q05_SYNE7
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–188; UniProt 13–200 Author chain J; PDBConstruct 1–188; UniProt 13–200 Author chain K; PDBConstruct 1–188; UniProt 13–200 Author chain L; PDBConstruct 1–188; UniProt 13–200 Author chain M; PDBConstruct 1–188; UniProt 13–200 Author chain N; PDBConstruct 1–188; UniProt 13–200 Author chain O; PDBConstruct 1–188; UniProt 13–200 Author chain P; PDBConstruct 1–188; UniProt 13–200

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 6smh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6smh
Deposition date deposition_date2019-08-21
Structure title titleCryo-electron microscopy structure of a RbcL-Raf1 supercomplex from Synechococcus elongatus PCC 7942
Keywords keywordsRubisco, Rubisco accumulation factor1, Raf1, Synechococcus elongatus 7942, Cyanobacteria, Photosynthesis; PHOTOSYNTHESIS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.51
Radius of gyration Rg (electron density) rg_electron50.76
Forward intensity I(0) i04600710000.00
Molecular weight molecular_weight563740.0 kDa
Excluded volume excluded_volume702280 ų
Envelope volume envelope_volume978250 ų
Hydration-shell volume shell_volume144460 ų
Envelope diameter envelope_diameter159.2
Shell Rg shell_rg64.60
Envelope Rg envelope_rg50.64
Shape Rg shape_rg50.78
Total Rg total_rg51.01
Total atoms total_atoms39744
Residues n_residues5025
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 dmax155.8
Rg (real space) rg_real51.20
Rg uncertainty (real space) rg_real_error0.71
I(0) (real space) i0_real4.6010e+09
I(0) uncertainty (real space) i0_real_error7.1730e+07
Rg (reciprocal space) rg_reciprocal51.77
I(0) (reciprocal space) i0_reciprocal4604000000.0000
Solution quality estimate total_estimate0.8848
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary70.3
Skewness Skewness skewness0.025
Kurtosis Kurtosis kurtosis-0.550
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha2479000000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.945; Smooth: 0.816

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)