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- PDB-9pmk: PhuZ Tubulin Tetramer from phage Goslar -

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Basic information

Entry
Database: PDB / ID: 9pmk
TitlePhuZ Tubulin Tetramer from phage Goslar
ComponentsTubulin/FtsZ GTPase domain-containing protein
KeywordsVIRAL PROTEIN / Phage / Tubulin / PhuZ
Function / homologyTubulin/FtsZ, GTPase domain superfamily / PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER / Tubulin/FtsZ GTPase domain-containing protein
Function and homology information
Biological speciesGoslarvirus
MethodELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 2.84 Å
AuthorsBasu, D. / Gu, Y. / Corbett, K.D.
Funding support United States, 1items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI)Emerging Pathogens Initiative United States
CitationJournal: To Be Published
Title: PhuZ Tubulin Tetramer from phage Goslar
Authors: Basu, D. / Gu, Y. / Corbett, K.D.
History
DepositionJul 17, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 24, 2025Provider: repository / Type: Initial release
Revision 1.0Dec 24, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Dec 24, 2025Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0Dec 24, 2025Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Dec 24, 2025Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Dec 24, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Dec 24, 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
C: Tubulin/FtsZ GTPase domain-containing protein
B: Tubulin/FtsZ GTPase domain-containing protein
A: Tubulin/FtsZ GTPase domain-containing protein
D: Tubulin/FtsZ GTPase domain-containing protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)144,7378
Polymers142,6524
Non-polymers2,0854
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein
Tubulin/FtsZ GTPase domain-containing protein


Mass: 35662.961 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: N-terminal SNA tag scar / Source: (gene. exp.) Goslarvirus / Gene: Goslar_00201 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A482GH76
#2: Chemical
ChemComp-G2P / PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER


Mass: 521.208 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C11H18N5O13P3 / Feature type: SUBJECT OF INVESTIGATION / Comment: GMP-CPP, energy-carrying molecule analogue*YM
Has ligand of interestY
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: FILAMENT / 3D reconstruction method: helical reconstruction

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Sample preparation

ComponentName: Tubulin PhuZ from Bacteriophage Goslar / Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: #1 / Source: RECOMBINANT
Source (natural)Organism: Goslarvirus
Source (recombinant)Organism: Escherichia coli (E. coli)
Details of virusType: VIRION
Buffer solutionpH: 7.4
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: 2000 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 55 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

EM software
IDNameCategory
1cryoSPARCparticle selection
2PHENIXmodel refinement
13cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Helical symmertyAngular rotation/subunit: -79.906 ° / Axial rise/subunit: 4.883 Å / Axial symmetry: C1
3D reconstructionResolution: 2.84 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 14671 / Symmetry type: HELICAL
RefinementHighest resolution: 2.84 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00410236
ELECTRON MICROSCOPYf_angle_d0.39613868
ELECTRON MICROSCOPYf_dihedral_angle_d10.4293836
ELECTRON MICROSCOPYf_chiral_restr0.0411540
ELECTRON MICROSCOPYf_plane_restr0.0041820

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