8i6v

Cryo-EM structure of the polyphosphate polymerase VTC complex(Vtc4/Vtc3/Vtc1)

Method: ELECTRON MICROSCOPY Dmax: 160.2 Å Quality: GOOD

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

Vacuolar transporter chaperone complex subunit 1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P40046

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–129 Chain B; UniProt 1–129 Chain C; UniProt 1–129 Not recorded Vacuolar transporter chaperone 3 complex subunit 3 × 1 (Q02725) Vacuolar transporter chaperone complex subunit 4 × 1 (P47075) POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 1 PO4 PHOSPHATE ION × 3 3PO TRIPHOSPHATE × 1 MN MANGANESE (II) ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.06 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 VTC1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–129; UniProt 1–129 Author chain B; PDBConstruct 1–129; UniProt 1–129 Author chain C; PDBConstruct 1–129; UniProt 1–129

Vacuolar transporter chaperone 3 complex subunit 3

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt Q02725

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 1–835 Not recorded Vacuolar transporter chaperone complex subunit 1 × 3 (P40046) Vacuolar transporter chaperone complex subunit 4 × 1 (P47075) POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 1 PO4 PHOSPHATE ION × 3 3PO TRIPHOSPHATE × 1 MN MANGANESE (II) ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.06 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 VTC3_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–835; UniProt 1–835

Vacuolar transporter chaperone complex subunit 4

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P47075

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 1–721 Not recorded Vacuolar transporter chaperone complex subunit 1 × 3 (P40046) Vacuolar transporter chaperone 3 complex subunit 3 × 1 (Q02725) POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 1 PO4 PHOSPHATE ION × 3 3PO TRIPHOSPHATE × 1 MN MANGANESE (II) ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.06 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.

10 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VTC4_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–721; UniProt 1–721

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 8i6v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8i6v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8i6v
Deposition date deposition_date2023-01-29
Structure title titleCryo-EM structure of the polyphosphate polymerase VTC complex(Vtc4/Vtc3/Vtc1)
Keywords keywordspolyphosphate polymerase; VTC complex; coupled synthesis and 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_guinier47.53
Radius of gyration Rg (electron density) rg_electron48.78
Forward intensity I(0) i0470061000.00
Molecular weight molecular_weight186400.0 kDa
Excluded volume excluded_volume236700 ų
Envelope volume envelope_volume340210 ų
Hydration-shell volume shell_volume62969 ų
Envelope diameter envelope_diameter170.2
Shell Rg shell_rg47.24
Envelope Rg envelope_rg48.03
Shape Rg shape_rg48.77
Total Rg total_rg48.74
Total atoms total_atoms13168
Residues n_residues1594
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 dmax160.2
Rg (real space) rg_real48.12
Rg uncertainty (real space) rg_real_error2.04
I(0) (real space) i0_real4.7010e+08
I(0) uncertainty (real space) i0_real_error1.0010e+07
Rg (reciprocal space) rg_reciprocal47.53
I(0) (reciprocal space) i0_reciprocal469700000.0000
Solution quality estimate total_estimate0.8073
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.7
Skewness Skewness skewness0.604
Kurtosis Kurtosis kurtosis-0.170
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha61760000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.798; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.920; Smooth: 0.176

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id8i6vE01
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology100 — mRNA Triphosphatase Cet1; Chain A
Homologous superfamily homologous superfamily30 — VTC, catalytic tunnel domain

8. Citations (1)

9. Files and Curves (10)