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- EMDB-15631: Cryo-EM reconstruction of the augmin TIII subcomplex -

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Basic information

Entry
Database: EMDB / ID: EMD-15631
TitleCryo-EM reconstruction of the augmin TIII subcomplex
Map dataCryo-EM reconstruction of the augmin TIII subcomplex
Sample
  • Complex: Augmin TIII subcomplex
    • Protein or peptide: HAUS augmin-like complex subunit 1
    • Protein or peptide: HAUS augmin-like complex subunit 3
    • Protein or peptide: HAUS augmin like complex subunit 4 L homeolog
    • Protein or peptide: HAUS augmin-like complex subunit 5
Function / homology
Function and homology information


HAUS complex / mitotic spindle microtubule / centrosome cycle / spindle assembly / spindle / microtubule / cell division / centrosome / cytoplasm
Similarity search - Function
HAUS augmin-like complex subunit 4, metazoa / HAUS complex subunit 5, metazoa / HAUS augmin-like complex subunit 1 / HAUS augmin-like complex subunit 5 / HAUS augmin-like complex subunit 4 / HAUS augmin-like complex subunit 4 / HAUS augmin-like complex subunit 5 / HAUS augmin-like complex subunit 3 / HAUS augmin-like complex subunit 3, N-terminal / HAUS augmin-like complex subunit 3
Similarity search - Domain/homology
HAUS augmin-like complex subunit 5 / LOC495502 protein / HAUS augmin like complex subunit 4 L homeolog / HAUS augmin-like complex subunit 3
Similarity search - Component
Biological speciesXenopus laevis (African clawed frog)
Methodsingle particle reconstruction / cryo EM / Resolution: 7.7 Å
AuthorsZupa E / Pfeffer S
Funding support Germany, 2 items
OrganizationGrant numberCountry
German Research Foundation (DFG)PF 963/1-4 Germany
German Research Foundation (DFG)Schi 295/4-4 Germany
CitationJournal: Nat Commun / Year: 2022
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
DepositionAug 22, 2022-
Header (metadata) releaseSep 28, 2022-
Map releaseSep 28, 2022-
UpdateOct 26, 2022-
Current statusOct 26, 2022Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_15631.png

Downloads & links

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Map

FileDownload / File: emd_15631.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCryo-EM reconstruction of the augmin TIII subcomplex
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
2.14 Å/pix.
x 256 pix.
= 547.84 Å		2.14 Å/pix.
x 256 pix.
= 547.84 Å		2.14 Å/pix.
x 256 pix.
= 547.84 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 2.14 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 1.31
Minimum - Maximum-1.974396 - 5.8148417
Average (Standard dev.)-0.0037578437 (±0.097772084)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 547.84 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Cryo-EM reconstruction of the augmin TIII subcomplex-half map A

Fileemd_15631_half_map_1.map
AnnotationCryo-EM reconstruction of the augmin TIII subcomplex-half map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Cryo-EM reconstruction of the augmin TIII subcomplex-half map B

Fileemd_15631_half_map_2.map
AnnotationCryo-EM reconstruction of the augmin TIII subcomplex-half map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Augmin TIII subcomplex

EntireName: Augmin TIII subcomplex
Components
  • Complex: Augmin TIII subcomplex
    • Protein or peptide: HAUS augmin-like complex subunit 1
    • Protein or peptide: HAUS augmin-like complex subunit 3
    • Protein or peptide: HAUS augmin like complex subunit 4 L homeolog
    • Protein or peptide: HAUS augmin-like complex subunit 5

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Supramolecule #1: Augmin TIII subcomplex

SupramoleculeName: Augmin TIII subcomplex / type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Xenopus laevis (African clawed frog)
Recombinant expressionOrganism: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)
Molecular weightTheoretical: 218 KDa

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Macromolecule #1: HAUS augmin-like complex subunit 1

MacromoleculeName: HAUS augmin-like complex subunit 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 32.684684 KDa
Recombinant expressionOrganism: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)
SequenceString: MDEKSTKIIM WLKKMFGDKP LPPYEVNTRT MEILYQLAEW NEARDKDLSL VTEDLKLKSA EVKAEAKYLQ DLLTEGLGPS YTNLSRMGN NYLNQIVDSC LALELKNSSL SSYIPAVNDL SSELVAIELN NQEMEAELTS LRKKLTEALV LEKSLERDLK K AEEQCNFE ...String:
MDEKSTKIIM WLKKMFGDKP LPPYEVNTRT MEILYQLAEW NEARDKDLSL VTEDLKLKSA EVKAEAKYLQ DLLTEGLGPS YTNLSRMGN NYLNQIVDSC LALELKNSSL SSYIPAVNDL SSELVAIELN NQEMEAELTS LRKKLTEALV LEKSLERDLK K AEEQCNFE KAKVEIRSQN MKKLKDKSEE YKYKIHAAKD QLSSAGMEEP LTHRSLVSLS ETLTELKAQS MAAKEKLNSY LD LAPNPSL VKVKIEEAKR ELKATEVELT TKVNMMEFVV PEPSKRRLK

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Macromolecule #2: HAUS augmin-like complex subunit 3

MacromoleculeName: HAUS augmin-like complex subunit 3 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 68.11225 KDa
Recombinant expressionOrganism: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)
SequenceString: MSGGDRFVQT LQKLNYPKGA QLDGEDFDWL FEAVDLKPFL DWFCSAASEQ NVVPDEKLQA FNTLKESGKP VLDEKALDEV LKTFSISKV PAIEEVAIEK LEEEVKALQK QKNLHIRRRN KLQMVESGNR QMCLKSKDKE EETGRAFQEV LHLLRVTNKK L NHELQSIV ...String:
MSGGDRFVQT LQKLNYPKGA QLDGEDFDWL FEAVDLKPFL DWFCSAASEQ NVVPDEKLQA FNTLKESGKP VLDEKALDEV LKTFSISKV PAIEEVAIEK LEEEVKALQK QKNLHIRRRN KLQMVESGNR QMCLKSKDKE EETGRAFQEV LHLLRVTNKK L NHELQSIV NGVQTLMSFF STPETACELS SQPIFLSQLL LDKYLSLEEQ STAALTSFTK EHFFEGMSKF VEGSDENFQL VQ LNVNSFG EDGTTEDKCK EMMRLQLAYI CAKHKLIQMK AKSASLKVGL QWAENNASVV QDKASQKEEN LKVRITSLKN ETL QIENHT NSISNEKLPG LVRDNAQLLN MPIVKGDYDL QMAHQTSCSS RQDLVCDHLM KQKASFELLQ LGYELELRKH RDVY RELGS IVQELKESGD KLEERLTMLS DVNLLSASKP RSNIDSKDLT SHRLYQLLDG DNTQKLFRTY DGLESVAQKL SQDIA SMRD QLEVSEQEHS LLLSKLDSHL KELRDFMYPE GNTLMLTTPE LSGEFHQLGS QLEKLNHITV EILGDLQLKR KMLESN KLQ QIEKQLYVYF FQNEEQLKSI VGKLEAQTGG GSSA

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Macromolecule #3: HAUS augmin like complex subunit 4 L homeolog

MacromoleculeName: HAUS augmin like complex subunit 4 L homeolog / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 41.256438 KDa
Recombinant expressionOrganism: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)
SequenceString: MAQTLQYVSS RLSMLQIDEE DLERNAQFGK VLIELCPLLG PNGGSANLNR ELEETRRELL LQRKMWMRSE VIYQLVQEML LDLQVRKLE GSLTEEERKF QDGLQQCMLV SECSRLLTAD SVPPSDSTSI LGLDKQDLLD LLPPNMLVLW VRDRLQKQLE E ALKKKCFT ...String:
MAQTLQYVSS RLSMLQIDEE DLERNAQFGK VLIELCPLLG PNGGSANLNR ELEETRRELL LQRKMWMRSE VIYQLVQEML LDLQVRKLE GSLTEEERKF QDGLQQCMLV SECSRLLTAD SVPPSDSTSI LGLDKQDLLD LLPPNMLVLW VRDRLQKQLE E ALKKKCFT FLSFHQPETD EEGDVLRAAK VLRLASTLED EKRRLQNEQE KHQEMRALLE KQQEIYPHVL LRCLSLLRQA AS ELRLRAQ SDIDRINAEY LEAKSNALFL KLRMEELQVL TDCYTPEKVL VHRQIRDTLE AGVKKEKQEL STSRQILSSY EFL GPEFEG LVQEYTRLKD KIKDNRWMLQ ELSKSLP

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Macromolecule #4: HAUS augmin-like complex subunit 5

MacromoleculeName: HAUS augmin-like complex subunit 5 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 77.357281 KDa
Recombinant expressionOrganism: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)
SequenceString: MERRSLAQEL KKWAVEEMGL PAQKAPSEEM LQRLFIGQCG DIWKFIIRHI HSHRTVRKIE GNLLWYQQLQ HTEAQRTAEE EQQQRRKQL CKEILELRAE LHHLQEQIQT AEREIVGQDL NCERAQDLCR RSLLLRAFNK KREEECEALC QSNKKIQYRC E QLQEIRRA ...String:
MERRSLAQEL KKWAVEEMGL PAQKAPSEEM LQRLFIGQCG DIWKFIIRHI HSHRTVRKIE GNLLWYQQLQ HTEAQRTAEE EQQQRRKQL CKEILELRAE LHHLQEQIQT AEREIVGQDL NCERAQDLCR RSLLLRAFNK KREEECEALC QSNKKIQYRC E QLQEIRRA SQREVMFSAV DPDLSSSTFL EPEVLRDVRE VCKLRFKFLR SLHDDSISSS VHPGKEDLRS LSHQQWMSMA EK VWNTHTP NHILAALERL TLNSTQELKK LQFSQAADLS KGPSCQLKEF SEPITQSRSC NESTHLDPQE TLPSFHSLIQ EGW ANSVKV SSELRRVQSQ AQALSEHLAE RIQEIHKKLS DGSEVSVLTR AAFDAELRCV ILRGCRDALM QECRMLQEEA AGKK QEMKL LQQQQQNIQE ACLLLDKKQK HIQILIKGNS SSKSQIRRSS VEAQKYVQDK LLPWPQEIIQ ESQRLQDSIQ KEVKH FSAI CLPALLKVST DGFNLLPSRE LSINRMSNTH APYYGIFKGI YESVRLPLYK APESVLSHVA DMKKQLFFLR SQLSSR SEA ISKTQRALQK NTNPDTDALL KSLSDHYSLE LDEMVPKMQR LIQQCEKHQE YGKEVQATVM DWWEQPVQLC LPSEERG GL TLRQWRERWT VAVTALQRAT GSRS

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
GridModel: Quantifoil R2/1 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 0.2 nm / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Atmosphere: OTHER
VitrificationCryogen name: ETHANE / Chamber humidity: 85 % / Chamber temperature: 298 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 81000
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 12615 / Average electron dose: 69.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 1060446
CTF correctionSoftware - Name: Gctf (ver. 1.06)
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3.2)
Final 3D classificationSoftware - Name: cryoSPARC (ver. 3.2)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3.2)
Final reconstructionNumber classes used: 5 / Applied symmetry - Point group: C1 (asymmetric) / Algorithm: BACK PROJECTION / Resolution.type: BY AUTHOR / Resolution: 7.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 3.2) / Number images used: 82776

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-8at2:
Structure of the augmin TIII subcomplex

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