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Open data
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Basic information
Entry | Database: PDB / ID: 8at4 | |||||||||
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Title | Structure of the augmin holocomplex in closed conformation | |||||||||
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![]() | CELL CYCLE / Microtubule / Branching / Nucleation | |||||||||
Function / homology | ![]() HAUS complex / mitotic spindle microtubule / microtubule minus-end binding / microtubule nucleation / centrosome cycle / spindle assembly / spindle pole / spindle / microtubule binding / microtubule ...HAUS complex / mitotic spindle microtubule / microtubule minus-end binding / microtubule nucleation / centrosome cycle / spindle assembly / spindle pole / spindle / microtubule binding / microtubule / cell division / centrosome / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / negative staining / Resolution: 33 Å | |||||||||
![]() | Zupa, E. / Pfeffer, S. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: The augmin complex architecture reveals structural insights into microtubule branching. Authors: Erik Zupa / Martin Würtz / Annett Neuner / Thomas Hoffmann / Mandy Rettel / Anna Böhler / Bram J A Vermeulen / Sebastian Eustermann / Elmar Schiebel / Stefan Pfeffer / ![]() Abstract: In mitosis, the augmin complex binds to spindle microtubules to recruit the γ-tubulin ring complex (γ-TuRC), the principal microtubule nucleator, for the formation of branched microtubules. Our ...In mitosis, the augmin complex binds to spindle microtubules to recruit the γ-tubulin ring complex (γ-TuRC), the principal microtubule nucleator, for the formation of branched microtubules. Our understanding of augmin-mediated microtubule branching is hampered by the lack of structural information on the augmin complex. Here, we elucidate the molecular architecture and conformational plasticity of the augmin complex using an integrative structural biology approach. The elongated structure of the augmin complex is characterised by extensive coiled-coil segments and comprises two structural elements with distinct but complementary functions in γ-TuRC and microtubule binding, linked by a flexible hinge. The augmin complex is recruited to microtubules via a composite microtubule binding site comprising a positively charged unordered extension and two calponin homology domains. Our study provides the structural basis for augmin function in branched microtubule formation, decisively fostering our understanding of spindle formation in mitosis. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 572.5 KB | Display | ![]() |
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PDB format | ![]() | 453.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 988.7 KB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 109.1 KB | Display | |
Data in CIF | ![]() | 158.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 15633MC ![]() 8at2C ![]() 8at3C M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
-HAUS augmin-like complex subunit ... , 4 types, 4 molecules ABDH
#1: Protein | Mass: 32684.684 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: Q3B8L5 |
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#2: Protein | Mass: 68112.250 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: Q6DCY9 |
#4: Protein | Mass: 77357.281 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: A0A1L8FPI2 |
#8: Protein | Mass: 41144.852 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: Q0IHJ3 |
-HAUS augmin like complex subunit ... , 4 types, 4 molecules CEFG
#3: Protein | Mass: 41256.438 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: Q4V7I1 |
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#5: Protein | Mass: 25135.715 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: Q6INL9 |
#6: Protein | Mass: 110863.484 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: A0JPI0 |
#7: Protein | Mass: 39379.605 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: B1H1T5 |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: Augmin octameric holocomplex / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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Molecular weight | Value: 0.435 MDa / Experimental value: NO |
Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: YES / Vitrification applied: NO |
EM staining | Type: NEGATIVE / Material: Uranyl Acetate |
Specimen support | Grid material: COPPER/PALLADIUM / Grid mesh size: 400 divisions/in. / Grid type: Quantifoil |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Talos L120C / Image courtesy: FEI Company |
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Microscopy | Model: TFS TALOS L120C |
Electron gun | Electron source: LAB6 / Accelerating voltage: 120 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 2000 nm |
Image recording | Electron dose: 101.8 e/Å2 / Film or detector model: FEI CETA (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 583 |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 80837 | ||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 33 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 10658 / Algorithm: BACK PROJECTION / Symmetry type: POINT | ||||||||||||||||||||||||||||||||
Atomic model building | Protocol: RIGID BODY FIT / Space: REAL |