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- PDB-7anz: Structure of the Candida albicans gamma-Tubulin Small Complex -

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Basic information

Entry
Database: PDB / ID: 7anz
TitleStructure of the Candida albicans gamma-Tubulin Small Complex
Components
  • (Spindle pole body component) x 2
  • Tubulin gamma chain
KeywordsCYTOSOLIC PROTEIN / gamma-Tubulin Small Complex / Cytoskeleton / Microtubule nucleation
Function / homology
Function and homology information


inner plaque of spindle pole body / microtubule nucleation by spindle pole body / outer plaque of spindle pole body / gamma-tubulin small complex / gamma-tubulin complex / microtubule nucleation / spindle pole body / gamma-tubulin binding / positive regulation of cytoplasmic translation / spindle assembly ...inner plaque of spindle pole body / microtubule nucleation by spindle pole body / outer plaque of spindle pole body / gamma-tubulin small complex / gamma-tubulin complex / microtubule nucleation / spindle pole body / gamma-tubulin binding / positive regulation of cytoplasmic translation / spindle assembly / cytoplasmic microtubule organization / mitotic spindle organization / meiotic cell cycle / structural constituent of cytoskeleton / spindle pole / mitotic cell cycle / microtubule / GTP binding / cytoplasm
Similarity search - Function
Gamma tubulin / Gamma tubulin complex component, C-terminal / Gamma-tubulin complex component, C-terminal domain superfamily / Gamma tubulin complex component C-terminal / Gamma-tubulin complex component protein / Gamma tubulin complex component protein, N-terminal / Gamma tubulin complex component N-terminal / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain ...Gamma tubulin / Gamma tubulin complex component, C-terminal / Gamma-tubulin complex component, C-terminal domain superfamily / Gamma tubulin complex component C-terminal / Gamma-tubulin complex component protein / Gamma tubulin complex component protein, N-terminal / Gamma tubulin complex component N-terminal / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily
Similarity search - Domain/homology
Spindle pole body component / Tubulin gamma chain / Spindle pole body component
Similarity search - Component
Biological speciesCandida albicans (yeast)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.6 Å
AuthorsZupa, E. / Pfeffer, S.
Funding support Germany, 1items
OrganizationGrant numberCountry
German Research Foundation (DFG)Schi 295/4-4 Germany
CitationJournal: Nat Commun / Year: 2020
Title: The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems.
Authors: Erik Zupa / Anjun Zheng / Annett Neuner / Martin Würtz / Peng Liu / Anna Böhler / Elmar Schiebel / Stefan Pfeffer /
Abstract: The nucleation of microtubules from αβ-tubulin subunits is mediated by γ-tubulin complexes, which vary in composition across organisms. Aiming to understand how de novo microtubule formation is ...The nucleation of microtubules from αβ-tubulin subunits is mediated by γ-tubulin complexes, which vary in composition across organisms. Aiming to understand how de novo microtubule formation is achieved and regulated by a minimal microtubule nucleation system, we here determined the cryo-electron microscopy structure of the heterotetrameric γ-tubulin small complex (γ-TuSC) from C. albicans at near-atomic resolution. Compared to the vertebrate γ-tubulin ring complex (γ-TuRC), we observed a vastly remodeled interface between the SPC/GCP-γ-tubulin spokes, which stabilizes the complex and defines the γ-tubulin arrangement. The relative positioning of γ-tubulin subunits indicates that a conformational rearrangement of the complex is required for microtubule nucleation activity, which follows opposing directionality as predicted for the vertebrate γ-TuRC. Collectively, our data suggest that the assembly and regulation mechanisms of γ-tubulin complexes fundamentally differ between the microtubule nucleation systems in lower and higher eukaryotes.
History
DepositionOct 13, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 4, 2020Provider: repository / Type: Initial release
Revision 1.1Nov 18, 2020Group: Database references / Category: citation
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Nov 25, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.3May 1, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / em_3d_fitting_list / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _em_3d_fitting_list.accession_code / _em_3d_fitting_list.initial_refinement_model_id / _em_3d_fitting_list.source_name / _em_3d_fitting_list.type

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Structure visualization

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  • Deposited structure unit
  • Imaged by Jmol
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  • Superimposition on EM map
  • EMDB-11835
  • Imaged by UCSF Chimera
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Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
B: Tubulin gamma chain
A: Tubulin gamma chain
C: Spindle pole body component
D: Spindle pole body component


Theoretical massNumber of molelcules
Total (without water)307,0224
Polymers307,0224
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: microscopy
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area14610 Å2
ΔGint-61 kcal/mol
Surface area90970 Å2
MethodPISA

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Components

#1: Protein Tubulin gamma chain / Gamma-tubulin


Mass: 56532.543 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Candida albicans (yeast) / Gene: TUB4 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: O93807
#2: Protein Spindle pole body component


Mass: 101660.453 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Candida albicans (yeast) / Gene: CAALFM_CR06740WA, orf19.708 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q59PZ2
#3: Protein Spindle pole body component


Mass: 92296.180 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Candida albicans (yeast) / Gene: SPC98, CAALFM_CR01990CA, orf19.2600 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: A0A1D8PS42

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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: gamma-Tubulin Small Complex / Type: COMPLEX
Details: Candida albicans gamma-Tubulin Small Complex expressed and purified from SF21 cells
Entity ID: all / Source: RECOMBINANT
Molecular weightValue: 0.3067 MDa / Experimental value: NO
Source (natural)Organism: Candida albicans (yeast)
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm)
Buffer solutionpH: 7.4
Buffer component
IDConc.UnitsNameFormulaBuffer-ID
150 mMTrisC4H11NO31
2mMSodium ChlorideNaCl1
30.5 mMEGTAC14H24N2O101
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: Gatan Solarus 950 plasma cleaner / Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R2/1
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 75 % / Chamber temperature: 298 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 3500 nm / Nominal defocus min: 2000 nm / Cs: 2.7 mm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 2.1 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 2 / Num. of real images: 1399
EM imaging opticsEnergyfilter slit width: 20 eV
Image scansWidth: 3710 / Height: 3838 / Movie frames/image: 20

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Processing

SoftwareName: PHENIX / Version: dev_3699: / Classification: refinement
EM software
IDNameVersionCategoryDetails
1RELION3particle selectionBeta version
2SerialEM3.7image acquisition
4Gctf1.06CTF correction
7UCSF Chimera1.13.1model fitting
8Coot0.9model fitting
10RELION3initial Euler assignmentBeta version
11RELION3final Euler assignmentBeta version
12RELION3classificationBeta version
13RELION33D reconstructionBeta version
14PHENIX1.14model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selectionNum. of particles selected: 1860000
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 274326 / Symmetry type: POINT
Atomic model building
IDPDB-ID 3D fitting-IDAccession codeInitial refinement model-IDSource nameType
13RIP

3rip

13RIP1PDBexperimental model
21Z5W

1z5w

11Z5W2PDBexperimental model
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00317112
ELECTRON MICROSCOPYf_angle_d0.7523108
ELECTRON MICROSCOPYf_dihedral_angle_d16.7972199
ELECTRON MICROSCOPYf_chiral_restr0.0462603
ELECTRON MICROSCOPYf_plane_restr0.0052931

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