6itc

Structure of a substrate engaged SecA-SecY protein translocation machine

Method: ELECTRON MICROSCOPY Dmax: 146.3 Å Quality: GOOD

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

Protein translocase subunit SecA

Bacillus subtilis (strain 168)

UniProt P28366

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–780 Not recorded Protein translocase subunit SecY × 1 (A4IJK8) Protein translocase subunit SecE × 1 (A4IJH4) Nanobody × 1 Translocating peptide × 1 Green fluorescent protein × 1 (P42212) Nanobody × 1 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.45 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.

16 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SECA_BACSU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–780; UniProt 1–780

Protein translocase subunit SecY

Geobacillus thermodenitrificans (strain NG80-2)

UniProt A4IJK8

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain Y; UniProt 1–430 Mutation:G60C,Q202T,L210G,F211G,R213N Protein translocase subunit SecA × 1 (P28366) Protein translocase subunit SecE × 1 (A4IJH4) Nanobody × 1 Translocating peptide × 1 Green fluorescent protein × 1 (P42212) Nanobody × 1 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.45 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A4IJK8_GEOTN
Isoform
PDB entities 2
Chains and sequence ranges Author chain Y; PDBConstruct 1–424; UniProt 1–430

Protein translocase subunit SecE

Geobacillus thermodenitrificans (strain NG80-2)

UniProt A4IJH4

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain E; UniProt 1–60 Not recorded Protein translocase subunit SecA × 1 (P28366) Protein translocase subunit SecY × 1 (A4IJK8) Nanobody × 1 Translocating peptide × 1 Green fluorescent protein × 1 (P42212) Nanobody × 1 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.45 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A4IJH4_GEOTN
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–60; UniProt 1–60

Green fluorescent protein

Aequorea victoria

UniProt P42212

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain G; UniProt 1–238 Mutation:Q80R,F99S,M153T,V163A Non-standard monomer:Yes (specific site not provided by mmCIF) Protein translocase subunit SecA × 1 (P28366) Protein translocase subunit SecY × 1 (A4IJK8) Protein translocase subunit SecE × 1 (A4IJH4) Nanobody × 1 Translocating peptide × 1 Nanobody × 1 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.45 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 6
Chains and sequence ranges Author chain G; PDBConstruct 1–236; UniProt 1–238

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 6itc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6itc
Deposition date deposition_date2018-11-21
Structure title titleStructure of a substrate engaged SecA-SecY protein translocation machine
Keywords keywordsSecA, SecY, Translocation, Cryo-EM, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.29
Radius of gyration Rg (electron density) rg_electron44.00
Forward intensity I(0) i0557590000.00
Molecular weight molecular_weight196710.0 kDa
Excluded volume excluded_volume247540 ų
Envelope volume envelope_volume339160 ų
Hydration-shell volume shell_volume66382 ų
Envelope diameter envelope_diameter158.0
Shell Rg shell_rg46.98
Envelope Rg envelope_rg43.33
Shape Rg shape_rg44.01
Total Rg total_rg44.10
Total atoms total_atoms13841
Residues n_residues1735
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 dmax146.3
Rg (real space) rg_real44.35
Rg uncertainty (real space) rg_real_error1.28
I(0) (real space) i0_real5.5760e+08
I(0) uncertainty (real space) i0_real_error1.0140e+07
Rg (reciprocal space) rg_reciprocal44.29
I(0) (reciprocal space) i0_reciprocal557500000.0000
Solution quality estimate total_estimate0.8700
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.8
Skewness Skewness skewness0.354
Kurtosis Kurtosis kurtosis-0.318
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha57310000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.906; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.597

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id6itcA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id6itcA02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1440 — Pre-protein croslinking domain of SecA
Homologous superfamily homologous superfamily10 — SecA, preprotein cross-linking domain
Domain ID domain_id6itcA03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id6itcA04
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology3060 — Helical scaffold and wing domains of SecA
Homologous superfamily homologous superfamily10 — Helical scaffold and wing domains of SecA

8. Citations (1)

9. Files and Curves (10)