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- PDB-9e2h: Variediene synthase hexameric prenyltransferase core -

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Basic information

Entry
Database: PDB / ID: 9e2h
TitleVariediene synthase hexameric prenyltransferase core
ComponentsVariediene synthase
KeywordsTRANSFERASE / Enzyme / terpene / bifunctional / variediene
Function / homology
Function and homology information


variediene synthase / (2E)-alpha-cericerene synthase / geranylfarnesyl diphosphate synthase / alcohol biosynthetic process / mycotoxin biosynthetic process / geranylgeranyl diphosphate synthase / prenyltransferase activity / terpenoid biosynthetic process / lyase activity / metal ion binding
Similarity search - Function
Terpene synthase family 2, C-terminal metal binding / Polyprenyl synthases signature 1. / Polyprenyl synthases signature 2. / Polyprenyl synthetase, conserved site / Polyprenyl synthetase / Polyprenyl synthetase / Isoprenoid synthase domain superfamily
Similarity search - Domain/homology
Biological speciesAspergillus stellatus (mold)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.77 Å
AuthorsWenger, E.S. / Christianson, D.W.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)574961-0089 United States
CitationJournal: To Be Published
Title: Variediene synthase hexameric prenyltransferase core
Authors: Wenger, E.S. / Christianson, D.W.
History
DepositionOct 22, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 21, 2025Provider: repository / Type: Initial release
Revision 1.0May 21, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0May 21, 2025Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0May 21, 2025Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0May 21, 2025Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0May 21, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0May 21, 2025Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Variediene synthase
B: Variediene synthase
C: Variediene synthase
D: Variediene synthase
E: Variediene synthase
F: Variediene synthase


Theoretical massNumber of molelcules
Total (without water)495,4226
Polymers495,4226
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein
Variediene synthase / VS


Mass: 82570.250 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Aspergillus stellatus (mold) / Gene: EvVS / Production host: Escherichia coli (E. coli)
References: UniProt: A0A0P0ZD79, variediene synthase, (2E)-alpha-cericerene synthase, geranylgeranyl diphosphate synthase, geranylfarnesyl diphosphate synthase
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Hexameric prenyltransferase core of variediene synthase from Emericella variecolor (EvVS)
Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Aspergillus stellatus (mold)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 800 nm
Image recordingElectron dose: 43 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM softwareName: PHENIX / Category: model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: C3 (3 fold cyclic)
3D reconstructionResolution: 2.77 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 491079 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00313296
ELECTRON MICROSCOPYf_angle_d0.61517950
ELECTRON MICROSCOPYf_dihedral_angle_d3.4911772
ELECTRON MICROSCOPYf_chiral_restr0.0382030
ELECTRON MICROSCOPYf_plane_restr0.0052342

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