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- EMDB-54160: D. melanogaster augmin TII N-clamp (GST-fusion) bound to a microtubule -

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Basic information

Entry
Database: EMDB / ID: EMD-54160
TitleD. melanogaster augmin TII N-clamp (GST-fusion) bound to a microtubule
Map dataD. melanogaster augmin TII N-clamp bound to 13PF microtubule.
Sample
  • Complex: D. melanogaster augmin TII N-clamp bound to a microtubule.
    • Complex: Taxol-stabilized microtubule.
    • Complex: D. melanogaster augmin TII N-clamp
KeywordsMicrotubules / microtubule nucleation / cell division / augmin / HAUS / CELL CYCLE
Function / homology
Function and homology information


mitotic spindle-templated microtubule nucleation / HAUS complex / mitotic spindle microtubule / motile cilium / regulation of mitotic nuclear division / glutathione transferase / centrosome duplication / glutathione transferase activity / mitotic spindle assembly / glutathione metabolic process ...mitotic spindle-templated microtubule nucleation / HAUS complex / mitotic spindle microtubule / motile cilium / regulation of mitotic nuclear division / glutathione transferase / centrosome duplication / glutathione transferase activity / mitotic spindle assembly / glutathione metabolic process / bioluminescence / mitotic spindle organization / generation of precursor metabolites and energy / kinetochore / structural constituent of cytoskeleton / microtubule cytoskeleton organization / spindle / neuron migration / spindle pole / mitotic cell cycle / protein-macromolecule adaptor activity / microtubule binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule / hydrolase activity / cell division / GTPase activity / centrosome / GTP binding / metal ion binding / cytoplasm
Similarity search - Function
HAUS augmin-like complex subunit 6 / HAUS augmin-like complex subunit 6, N-terminal / HAUS augmin-like complex subunit 6 N-terminus / Glutathione S-transferase, C-terminal domain / : / Glutathione S-transferase, N-terminal domain / Glutathione transferase family / Glutathione S-transferase, C-terminal / Glutathione S-transferase, C-terminal-like / Soluble glutathione S-transferase C-terminal domain profile. ...HAUS augmin-like complex subunit 6 / HAUS augmin-like complex subunit 6, N-terminal / HAUS augmin-like complex subunit 6 N-terminus / Glutathione S-transferase, C-terminal domain / : / Glutathione S-transferase, N-terminal domain / Glutathione transferase family / Glutathione S-transferase, C-terminal / Glutathione S-transferase, C-terminal-like / Soluble glutathione S-transferase C-terminal domain profile. / Soluble glutathione S-transferase N-terminal domain profile. / Glutathione S-transferase, N-terminal / Glutathione S-transferase, C-terminal domain superfamily / Tubulin-beta mRNA autoregulation signal. / Alpha tubulin / Beta tubulin, autoregulation binding site / Beta tubulin / Green fluorescent protein, GFP / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Green fluorescent protein-related / Green fluorescent protein / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / Green fluorescent protein / 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 / Thioredoxin-like superfamily
Similarity search - Domain/homology
Tubulin alpha-1A chain / Tubulin beta chain / Glutathione S-transferase class-mu 26 kDa isozyme / Green fluorescent protein / Augmin complex subunit dgt6 / Augmin complex subunit msd5 / Augmin complex subunit dgt4
Similarity search - Component
Biological speciesDrosophila melanogaster (fruit fly) / Sus scrofa (pig)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.9 Å
AuthorsWuertz M / Vermeulen BJA / Tonon G / Pfeffer S
Funding support Germany, 9 items
OrganizationGrant numberCountry
German Research Foundation (DFG)DFG Schi 295/4-4 Germany
German Research Foundation (DFG)DFG SCHI 295/11-1 Germany
German Research Foundation (DFG)DFG SCHI 295/9-1 Germany
German Research Foundation (DFG)DFG PF 963/1-4 Germany
German Research Foundation (DFG)DFG PF 963/4-1 Germany
German Research Foundation (DFG)Sch Baden-Wuerttemberg Germany
German Research Foundation (DFG)INST 35/1314-1 FUGG Germany
German Research Foundation (DFG)INST 35/1503-1 FUGG Germany
German Research Foundation (DFG)INST 35/1134-1 FUGG Germany
CitationJournal: To Be Published / Year: 2025
Title: Structural insights into the augmin-microtubule interaction reveal a conserved function of the HAUS6 CH domain in orienting augmin on microtubules
Authors: Wuertz M / Tonon G / Vermeulen BJA / Zezlina M / Gao G / Annett N / Seidl A / Koenig M / Harkenthal M / Eustermann S / Erhardt S / Lolicato F / Schiebel E / Pfeffer S
History
DepositionJun 24, 2025-
Header (metadata) releaseAug 27, 2025-
Map releaseAug 27, 2025-
UpdateAug 27, 2025-
Current statusAug 27, 2025Processing site: PDBe / Status: Released

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Structure visualization

Downloads & links

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Map

FileDownload / File: emd_54160.map.gz / Format: CCP4 / Size: 307.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationD. melanogaster augmin TII N-clamp bound to 13PF microtubule.
Voxel sizeX=Y=Z: 1.069 Å
Density
Contour LevelBy AUTHOR: 0.185
Minimum - Maximum-0.39606693 - 0.9421287
Average (Standard dev.)0.00085490884 (±0.018979162)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions432432432
Spacing432432432
CellA=B=C: 461.808 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : D. melanogaster augmin TII N-clamp bound to a microtubule.

EntireName: D. melanogaster augmin TII N-clamp bound to a microtubule.
Components
  • Complex: D. melanogaster augmin TII N-clamp bound to a microtubule.
    • Complex: Taxol-stabilized microtubule.
    • Complex: D. melanogaster augmin TII N-clamp

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Supramolecule #1: D. melanogaster augmin TII N-clamp bound to a microtubule.

SupramoleculeName: D. melanogaster augmin TII N-clamp bound to a microtubule.
type: complex / ID: 1 / Parent: 0
Source (natural)Organism: Drosophila melanogaster (fruit fly)

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Supramolecule #2: Taxol-stabilized microtubule.

SupramoleculeName: Taxol-stabilized microtubule. / type: complex / ID: 2 / Parent: 1
Source (natural)Organism: Sus scrofa (pig) / Organ: Brain

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Supramolecule #3: D. melanogaster augmin TII N-clamp

SupramoleculeName: D. melanogaster augmin TII N-clamp / type: complex / ID: 3 / Parent: 1
Source (natural)Organism: Drosophila melanogaster (fruit fly)

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation statehelical array

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Sample preparation

BufferpH: 6.8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 40.4 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: Gctf / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
In silico model: Synthetic reference provided under https://github.com/moores-lab/MiRPv2/tree/main/data/protofilament_sorting_references
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.4.1) / Number images used: 457096
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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