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- EMDB-11888: Recombinant human gTuRC -

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Basic information

Entry
Database: EMDB / ID: EMD-11888
TitleRecombinant human gTuRC
Map dataConsensus map
Sample
  • Complex: Recombinant human gamma-tubulin ring complex
    • Protein or peptide: Tubulin gamma-1 chain
    • Protein or peptide: Gamma-tubulin complex component 3
    • Protein or peptide: Gamma-tubulin complex component 6
    • Protein or peptide: Mitotic-spindle organizing protein 1
    • Protein or peptide: Actin, cytoplasmic 1
    • Protein or peptide: Gamma-tubulin complex component 2
    • Protein or peptide: Gamma-tubulin complex component 4
    • Protein or peptide: Gamma-tubulin complex component 5
  • Ligand: GUANOSINE-5'-DIPHOSPHATE
Function / homology
Function and homology information


microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / positive regulation of norepinephrine uptake / equatorial microtubule organizing center / cellular response to cytochalasin B / bBAF complex / mitotic spindle microtubule / gamma-tubulin ring complex / interphase microtubule organizing center / npBAF complex ...microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / positive regulation of norepinephrine uptake / equatorial microtubule organizing center / cellular response to cytochalasin B / bBAF complex / mitotic spindle microtubule / gamma-tubulin ring complex / interphase microtubule organizing center / npBAF complex / postsynaptic actin cytoskeleton organization / regulation of transepithelial transport / brahma complex / polar microtubule / nBAF complex / structural constituent of postsynaptic actin cytoskeleton / gamma-tubulin complex / morphogenesis of a polarized epithelium / Formation of annular gap junctions / meiotic spindle organization / GBAF complex / Gap junction degradation / postsynaptic actin cytoskeleton / protein localization to adherens junction / regulation of G0 to G1 transition / dense body / Cell-extracellular matrix interactions / Tat protein binding / Folding of actin by CCT/TriC / regulation of double-strand break repair / microtubule nucleation / regulation of nucleotide-excision repair / RSC-type complex / apical protein localization / Prefoldin mediated transfer of substrate to CCT/TriC / adherens junction assembly / non-motile cilium / RHOF GTPase cycle / gamma-tubulin binding / Adherens junctions interactions / tight junction / Sensory processing of sound by outer hair cells of the cochlea / SWI/SNF complex / Interaction between L1 and Ankyrins / Sensory processing of sound by inner hair cells of the cochlea / regulation of mitotic metaphase/anaphase transition / regulation of norepinephrine uptake / positive regulation of double-strand break repair / positive regulation of T cell differentiation / microtubule organizing center / NuA4 histone acetyltransferase complex / regulation of synaptic vesicle endocytosis / apical junction complex / maintenance of blood-brain barrier / establishment or maintenance of cell polarity / cortical cytoskeleton / positive regulation of double-strand break repair via homologous recombination / positive regulation of stem cell population maintenance / pericentriolar material / nitric-oxide synthase binding / single fertilization / Recycling pathway of L1 / regulation of cyclin-dependent protein serine/threonine kinase activity / cell leading edge / regulation of G1/S transition of mitotic cell cycle / mitotic sister chromatid segregation / negative regulation of cell differentiation / brush border / kinesin binding / calyx of Held / EPH-ephrin mediated repulsion of cells / mitotic spindle assembly / RHO GTPases Activate WASPs and WAVEs / spindle assembly / RHO GTPases activate IQGAPs / positive regulation of myoblast differentiation / cytoplasmic microtubule / regulation of protein localization to plasma membrane / cytoplasmic microtubule organization / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / Recruitment of NuMA to mitotic centrosomes / EPHB-mediated forward signaling / Anchoring of the basal body to the plasma membrane / substantia nigra development / centriole / axonogenesis / AURKA Activation by TPX2 / mitotic spindle organization / ciliary basal body / meiotic cell cycle / negative regulation of protein binding / condensed nuclear chromosome / actin filament / cell motility / RHO GTPases Activate Formins / Translocation of SLC2A4 (GLUT4) to the plasma membrane / regulation of transmembrane transporter activity / positive regulation of cell differentiation
Similarity search - Function
Mitotic-spindle organizing protein 1 / Mitotic-spindle organizing gamma-tubulin ring associated / Gamma-tubulin complex component 6, N-terminal / Gamma-tubulin complex component 6 N-terminus / 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 ...Mitotic-spindle organizing protein 1 / Mitotic-spindle organizing gamma-tubulin ring associated / Gamma-tubulin complex component 6, N-terminal / Gamma-tubulin complex component 6 N-terminus / 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 / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / 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 / ATPase, nucleotide binding domain
Similarity search - Domain/homology
Tubulin gamma-1 chain / Actin, cytoplasmic 1 / Mitotic-spindle organizing protein 1 / Gamma-tubulin complex component 3 / Gamma-tubulin complex component 6 / Gamma-tubulin complex component 5 / Gamma-tubulin complex component 2 / Gamma-tubulin complex component 4
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.13 Å
AuthorsSerna M / Fernandez-Leiro R / Llorca O
Funding support Spain, 3 items
OrganizationGrant numberCountry
Spanish Ministry of Science, Innovation, and UniversitiesSAF2017-82632-P Spain
Other governmentP2018/NMT4443 Spain
Other governmentY2018/BIO4747 Spain
CitationJournal: Sci Adv / Year: 2020
Title: Assembly of the asymmetric human γ-tubulin ring complex by RUVBL1-RUVBL2 AAA ATPase.
Authors: Fabian Zimmermann / Marina Serna / Artur Ezquerra / Rafael Fernandez-Leiro / Oscar Llorca / Jens Luders /
Abstract: The microtubule nucleator γ-tubulin ring complex (γTuRC) is essential for the function of microtubule organizing centers such as the centrosome. Since its discovery over two decades ago, γTuRC has ...The microtubule nucleator γ-tubulin ring complex (γTuRC) is essential for the function of microtubule organizing centers such as the centrosome. Since its discovery over two decades ago, γTuRC has evaded in vitro reconstitution and thus detailed structure-function studies. Here, we show that a complex of RuvB-like protein 1 (RUVBL1) and RUVBL2 "RUVBL" controls assembly and composition of γTuRC in human cells. Likewise, RUVBL assembles γTuRC from a minimal set of core subunits in a heterologous coexpression system. RUVBL interacts with γTuRC subcomplexes but is not part of fully assembled γTuRC. Purified, reconstituted γTuRC has nucleation activity and resembles native γTuRC as revealed by its cryo-electron microscopy (cryo-EM) structure at ~4.0-Å resolution. We further use cryo-EM to identify features that determine the intricate, higher-order γTuRC architecture. Our work finds RUVBL as an assembly factor that regulates γTuRC in cells and allows production of recombinant γTuRC for future in-depth mechanistic studies.
History
DepositionOct 26, 2020-
Header (metadata) releaseJan 20, 2021-
Map releaseJan 20, 2021-
UpdateJan 20, 2021-
Current statusJan 20, 2021Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.012
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.012
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7as4
  • Surface level: 0.012
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_11888.png

Downloads & links

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Map

FileDownload / File: emd_11888.map.gz / Format: CCP4 / Size: 226.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationConsensus map
Voxel sizeX=Y=Z: 1.40862 Å
Density
Contour LevelBy AUTHOR: 0.007 / Movie #1: 0.012
Minimum - Maximum-0.00815065 - 0.055173773
Average (Standard dev.)-0.00011615107 (±0.002606626)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions390390390
Spacing390390390
CellA=B=C: 549.35986 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.40861538461541.40861538461541.4086153846154
M x/y/z390390390
origin x/y/z0.0000.0000.000
length x/y/z549.360549.360549.360
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS390390390
D min/max/mean-0.0080.055-0.000

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Supplemental data

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Additional map: Subvolume positions 1 to 3 half map 2

Fileemd_11888_additional_1.map
AnnotationSubvolume positions 1 to 3 half map 2
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Additional map: Subvolume positions 5 to 7 half map 1

Fileemd_11888_additional_10.map
AnnotationSubvolume positions 5 to 7 half map 1
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Additional map: Subvolume positions 4 to 6 half map 2

Fileemd_11888_additional_11.map
AnnotationSubvolume positions 4 to 6 half map 2
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Additional map: Subvolume positions 5 to 7

Fileemd_11888_additional_12.map
AnnotationSubvolume positions 5 to 7
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Additional map: Subvolume positions 5 to 7 half map 2

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Additional map: Subvolume positions 4 to 6 half map 1

Fileemd_11888_additional_14.map
AnnotationSubvolume positions 4 to 6 half map 1
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Additional map: Subvolume positions 4 to 6

Fileemd_11888_additional_15.map
AnnotationSubvolume positions 4 to 6
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Additional map: Subvolume positions 9 to 11 half map 1

Fileemd_11888_additional_16.map
AnnotationSubvolume positions 9 to 11 half map 1
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Additional map: Subvolume positions 9 to 11 half map 2

Fileemd_11888_additional_17.map
AnnotationSubvolume positions 9 to 11 half map 2
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Additional map: Subvolume positions 9 to 11

Fileemd_11888_additional_18.map
AnnotationSubvolume positions 9 to 11
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Additional map: Subvolume positions 8 to 10 half map 2

Fileemd_11888_additional_19.map
AnnotationSubvolume positions 8 to 10 half map 2
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Additional map: Subvolume positions 1 to 3 half map 1

Fileemd_11888_additional_2.map
AnnotationSubvolume positions 1 to 3 half map 1
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Additional map: Subvolume positions 7 to 9 half map 1

Fileemd_11888_additional_20.map
AnnotationSubvolume positions 7 to 9 half map 1
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Additional map: Subvolume positions 7 to 9 half map 2

Fileemd_11888_additional_21.map
AnnotationSubvolume positions 7 to 9 half map 2
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Additional map: Subvolume positions 8 to 10

Fileemd_11888_additional_22.map
AnnotationSubvolume positions 8 to 10
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Additional map: Subvolume positions 8 to 10 half map 1

Fileemd_11888_additional_23.map
AnnotationSubvolume positions 8 to 10 half map 1
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Additional map: Subvolume positions 6 to 8 half map 2

Fileemd_11888_additional_24.map
AnnotationSubvolume positions 6 to 8 half map 2
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Additional map: Subvolume positions 6 to 8

Fileemd_11888_additional_25.map
AnnotationSubvolume positions 6 to 8
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Additional map: Subvolume positions 6 to 8 half map 1

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AnnotationSubvolume positions 6 to 8 half map 1
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Additional map: Subvolume positions 7 to 9

Fileemd_11888_additional_27.map
AnnotationSubvolume positions 7 to 9
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Additional map: Subvolume positions 11 to 14 half map 1

Fileemd_11888_additional_28.map
AnnotationSubvolume positions 11 to 14 half map 1
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Additional map: Subvolume positions 11 to 14 half map 2

Fileemd_11888_additional_29.map
AnnotationSubvolume positions 11 to 14 half map 2
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Additional map: Subvolume positions 1 to 3

Fileemd_11888_additional_3.map
AnnotationSubvolume positions 1 to 3
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Additional map: Subvolume positions 11 to 14

Fileemd_11888_additional_30.map
AnnotationSubvolume positions 11 to 14
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Additional map: Subvolume positions 10 to 12 half map 2

Fileemd_11888_additional_31.map
AnnotationSubvolume positions 10 to 12 half map 2
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Additional map: Subvolume positions 10 to 12 half map 1

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Additional map: Subvolume positions 10 to 12

Fileemd_11888_additional_33.map
AnnotationSubvolume positions 10 to 12
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Additional map: Subvolume luminal bridge half map 2

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AnnotationSubvolume luminal bridge half map 2
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Additional map: Subvolume luminal bridge

Fileemd_11888_additional_35.map
AnnotationSubvolume luminal bridge
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Additional map: Subvolume luminal bridge half map 1

Fileemd_11888_additional_36.map
AnnotationSubvolume luminal bridge half map 1
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Additional map: Subvolume positions 2 to 4

Fileemd_11888_additional_4.map
AnnotationSubvolume positions 2 to 4
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Additional map: Subvolume positions 2 to 4 half map 2

Fileemd_11888_additional_5.map
AnnotationSubvolume positions 2 to 4 half map 2
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Additional map: Subvolume positions 2 to 4 half map 1

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AnnotationSubvolume positions 2 to 4 half map 1
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Additional map: Subvolume positions 3 to 5 half map 1

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AnnotationSubvolume positions 3 to 5 half map 1
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Additional map: Subvolume positions 3 to 5

Fileemd_11888_additional_8.map
AnnotationSubvolume positions 3 to 5
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Additional map: Subvolume positions 3 to 5 half map 2

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AnnotationSubvolume positions 3 to 5 half map 2
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Half map: Consensus half map 2

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AnnotationConsensus half map 2
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Half map: Consensus half map 1

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AnnotationConsensus half map 1
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Sample components

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Entire : Recombinant human gamma-tubulin ring complex

EntireName: Recombinant human gamma-tubulin ring complex
Components
  • Complex: Recombinant human gamma-tubulin ring complex
    • Protein or peptide: Tubulin gamma-1 chain
    • Protein or peptide: Gamma-tubulin complex component 3
    • Protein or peptide: Gamma-tubulin complex component 6
    • Protein or peptide: Mitotic-spindle organizing protein 1
    • Protein or peptide: Actin, cytoplasmic 1
    • Protein or peptide: Gamma-tubulin complex component 2
    • Protein or peptide: Gamma-tubulin complex component 4
    • Protein or peptide: Gamma-tubulin complex component 5
  • Ligand: GUANOSINE-5'-DIPHOSPHATE

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Supramolecule #1: Recombinant human gamma-tubulin ring complex

SupramoleculeName: Recombinant human gamma-tubulin ring complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm) / Recombinant plasmid: pBIG2

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Macromolecule #1: Tubulin gamma-1 chain

MacromoleculeName: Tubulin gamma-1 chain / type: protein_or_peptide / ID: 1 / Number of copies: 14 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 50.741297 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY IPRAVLLDLE PRVIHSILNS PYAKLYNPE NIYLSEHGGG AGNNWASGFS QGEKIHEDIF DIIDREADGS DSLEGFVLCH SIAGGTGSGL GSYLLERLND R YPKKLVQT ...String:
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY IPRAVLLDLE PRVIHSILNS PYAKLYNPE NIYLSEHGGG AGNNWASGFS QGEKIHEDIF DIIDREADGS DSLEGFVLCH SIAGGTGSGL GSYLLERLND R YPKKLVQT YSVFPNQDEM SDVVVQPYNS LLTLKRLTQN ADCVVVLDNT ALNRIATDRL HIQNPSFSQI NQLVSTIMSA ST TTLRYPG YMNNDLIGLI ASLIPTPRLH FLMTGYTPLT TDQSVASVRK TTVLDVMRRL LQPKNVMVST GRDRQTNHCY IAI LNIIQG EVDPTQVHKS LQRIRERKLA NFIPWGPASI QVALSRKSPY LPSAHRVSGL MMANHTSISS LFERTCRQYD KLRK REAFL EQFRKEDMFK DNFDEMDTSR EIVQQLIDEY HAATRPDYIS WG

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Macromolecule #2: Gamma-tubulin complex component 3

MacromoleculeName: Gamma-tubulin complex component 3 / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 103.710102 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MATPDQKSPN VLLQNLCCRI LGRSEADVAQ QFQYAVRVIG SNFAPTVERD EFLVAEKIKK ELIRQRREAD AALFSELHRK LHSQGVLKN KWSILYLLLS LSEDPRRQPS KVSSYATLFA QALPRDAHST PYYYARPQTL PLSYQDRSAQ SAQSSGSVGS S GISSIGLC ...String:
MATPDQKSPN VLLQNLCCRI LGRSEADVAQ QFQYAVRVIG SNFAPTVERD EFLVAEKIKK ELIRQRREAD AALFSELHRK LHSQGVLKN KWSILYLLLS LSEDPRRQPS KVSSYATLFA QALPRDAHST PYYYARPQTL PLSYQDRSAQ SAQSSGSVGS S GISSIGLC ALSGPAPAPQ SLLPGQSNQA PGVGDCLRQQ LGSRLAWTLT ANQPSSQATT SKGVPSAVSR NMTRSRREGD TG GTMEITE AALVRDILYV FQGIDGKNIK MNNTENCYKV EGKANLSRSL RDTAVRLSEL GWLHNKIRRY TDQRSLDRSF GLV GQSFCA ALHQELREYY RLLSVLHSQL QLEDDQGVNL GLESSLTLRR LLVWTYDPKI RLKTLAALVD HCQGRKGGEL ASAV HAYTK TGDPYMRSLV QHILSLVSHP VLSFLYRWIY DGELEDTYHE FFVASDPTVK TDRLWHDKYT LRKSMIPSFM TMDQS RKVL LIGKSINFLH QVCHDQTPTT KMIAVTKSAE SPQDAADLFT DLENAFQGKI DAAYFETSKY LLDVLNKKYS LLDHMQ AMR RYLLLGQGDF IRHLMDLLKP ELVRPATTLY QHNLTGILET AVRATNAQFD SPEILRRLDV RLLEVSPGDT GWDVFSL DY HVDGPIATVF TRECMSHYLR VFNFLWRAKR MEYILTDIRK GHMCNAKLLR NMPEFSGVLH QCHILASEMV HFIHQMQY Y ITFEVLECSW DELWNKVQQA QDLDHIIAAH EVFLDTIISR CLLDSDSRAL LNQLRAVFDQ IIELQNAQDA IYRAALEEL QRRLQFEEKK KQREIEGQWG VTAAEEEEEN KRIGEFKESI PKMCSQLRIL THFYQGIVQQ FLVLLTTSSD ESLRFLSFRL DFNEHYKAR EPRLRVSLGT RGRRSSHT

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Macromolecule #3: Gamma-tubulin complex component 6

MacromoleculeName: Gamma-tubulin complex component 6 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 200.733641 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MASITQLFDD LCEALLPAAK THLGQRSVNR KRAKRSLKKV AYNALFTNLF QDETQQLQPD MSKLPARNKI LMLSFDLRVG GLGPKADRL EELVEELEAA PCCPLLEVGS VLDLLVQLAG SGPPQVLPRK RDYFLNNKHV GRNVPYSGYD CDDLSVFEMD V QSLISREE ...String:
MASITQLFDD LCEALLPAAK THLGQRSVNR KRAKRSLKKV AYNALFTNLF QDETQQLQPD MSKLPARNKI LMLSFDLRVG GLGPKADRL EELVEELEAA PCCPLLEVGS VLDLLVQLAG SGPPQVLPRK RDYFLNNKHV GRNVPYSGYD CDDLSVFEMD V QSLISREE CLCHSMIQET LQVMEAAPGT GLPTVGLFSF GDPCGDRFER DTRVSLFGAL VHSRTYDMDV RLGLPPVPDN AD LSGLAIK VPPSVDQWED EGFQSASNLT PDSQSEPSVT PDVDLWEAAL TYEASKRRCW ERVGCPPGHR EEPYLTEAGR DAF DKFCRL HQGELQLLAG GVLQAPQPVL VKECELVKDV LNVLIGVVSA TFSLCQPAQA FVVKRGVHVS GASPESISSL LSEV AEYGT CYTRLSHFSL QPVLDSLYSK GLVFQAFTSG LRRYLQYYRA CVLSTPPTLS LLTIGFLFKK LGRQLRYLAE LCGVG AVLP GTCGGGPRAA FPTGVKLLSY LYQEALHNCS NEHYPVLLSL LKTSCEPYTR FIHDWVYSGV FRDAYGEFMI QVNHEY LSF RDKLYWTHGY VLISKEVEDC VPVFLKHIAH DIYVCGKTIN LLKLCCPRHY LCWSDVPVPR ISVIFSLEEL KEIEKDC AV YVGRMERVAR HSSVSKEEKE LRMEIAKQEL IAHAREAASR VLSALSDRQM SERMALDARK REQFQRLKEQ FVKDQERR Q AARQEELDDD FSYARELRDR ERRLKSLEEE LERKARQALV DHYSKLSAEA ARREQKALWR IQRHRLESAR LRFLLEDEK HIQEMLKAVS EAHQPQEPPD VLLSVHPQVT SPGPEHPEGG QGCDSGSAEQ HSPAWDGWNR PGLLTPQPLK PLAVGAGGRG LQQAEGARP FSDSLSIGDF LPVGPGAEPS VQTGMVPLLE VALQTINLDL PPSAPGEAPA AASTQPSRPQ EYDFSTVLRP A VATSPAPG PLQAAECSLG SSGLQLWEDS CGKMDACGSA SRETLLPSHP PRRAALEEGS SQPTERLFGQ VSGGGLPTGD YA SEIAPTR PRWNTHGHVS DASIRVGENV SDVAPTQPRW NTHGHVSNAS ISLGESVSDV APTRPRWNIH GHVSNASIRV GEN VSDVAP TRPRWNTHGH VSNASIRVGE NVSDVAPTRP RWNTHGHVSD ASISLGESVS DMAPARPRWN THGHVSDASI SLGE SVSDM APTRPRWNTH GHVSDTSIRV GENVSDVAPI RSRCNTHGHV SDASISLGEP VSDVVSTRPR WNTHVPIPPP HMVLG ALSP EAEPNTPRPQ QSPPGHTSQS ALSLGAQSTV LDCGPRLPVE VGPSLSSPSS GCGEGSISVG ENVSDVAPTQ PWWPNT PGD SVSEELGPGR SGDTEDLSPN WPLNSQEDTA AQSSPGRGEE AEASAAEAQG GEQAYLAGLA GQYHLERYPD SYESMSE PP IAHLLRPVLP RAFAFPVDPQ VQSAADETAV QLSELLTLPV LMKRSITAPL AAHISLVNKA AVDYFFVELH LEAHYEAL R HFLLMEDGEF AQSLSDLLFE KLGAGQTPGE LLNPLVLNSV LSKALQCSLH GDTPHASNLS LALKYLPEVF APNAPDVLS CLELRYKVDW PLNIVITEGC VSKYSGVFSF LLQLKLMMWA LKDVCFHLKR TALLSHMAGS VQFRQLQLFK HEMQHFVKVI QGYIANQIL HVTWCEFRAR LATVGDLEEI QRAHAEYLHK AVFRGLLTEK AAPVMNVIHS IFSLVLKFRS QLISQAWGPP G GPRGAEHP NFALMQQSYN TFKYYSHFLF KVVTKLVNRG YQPHLEDFLL RINFNNYYQD A

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Macromolecule #4: Mitotic-spindle organizing protein 1

MacromoleculeName: Mitotic-spindle organizing protein 1 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.485724 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MASSSGAGAA AAAAAANLNA VRETMDVLLE ISRILNTGLD METLSICVRL CEQGINPEAL SSVIKELRKA TEALKAAENM TS

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Macromolecule #5: Actin, cytoplasmic 1

MacromoleculeName: Actin, cytoplasmic 1 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.723527 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: DEEVAALVVD NGSGMCKAGF AGDDAPRAVF PSIVGRPRHQ GVMVGMGQKD SYVGDEAQSK RGILTLKYPI EHGIVTNWDD MEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVLDSGDGVS H TVPIYEGY ...String:
DEEVAALVVD NGSGMCKAGF AGDDAPRAVF PSIVGRPRHQ GVMVGMGQKD SYVGDEAQSK RGILTLKYPI EHGIVTNWDD MEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVLDSGDGVS H TVPIYEGY ALPHAILRLD LAGRDLTDYL MKILTERGYS FTTTEEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLEKS YE LKDGQVI TIGNERFRCP EALFQPSFLG MEACGIHETT YNSIMKCDVD IRKDLYANTV LSGGTTMYPG IADRMQKEIT ALA PSTMKI KIIAPPERKY SVWIGGSILA SLSTFQQMWI SKQEYDESGP SIVHRKCF

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Macromolecule #6: Gamma-tubulin complex component 2

MacromoleculeName: Gamma-tubulin complex component 2 / type: protein_or_peptide / ID: 6 / Number of copies: 5 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 102.666953 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MSEFRIHHDV NELLSLLRVH GGDGAEVYID LLQKNRTPYV TTTVSAHSAK VKIAEFSRTP EDFLKKYDEL KSKNTRNLDP LVYLLSKLT EDKETLQYLQ QNAKERAELA AAAVGSSTTS INVPAAASKI SMQELEELRK QLGSVATGST LQQSLELKRK M LRDKQNKK ...String:
MSEFRIHHDV NELLSLLRVH GGDGAEVYID LLQKNRTPYV TTTVSAHSAK VKIAEFSRTP EDFLKKYDEL KSKNTRNLDP LVYLLSKLT EDKETLQYLQ QNAKERAELA AAAVGSSTTS INVPAAASKI SMQELEELRK QLGSVATGST LQQSLELKRK M LRDKQNKK NSGQHLPIFP AWVYERPALI GDFLIGAGIS TDTALPIGTL PLASQESAVV EDLLYVLVGV DGRYVSAQPL AG RQSRTFL VDPNLDLSIR ELVHRILPVA ASYSAVTRFI EEKSSFEYGQ VNHALAAAMR TLVKEHLILV SQLEQLHRQG LLS LQKLWF YIQPAMRTMD ILASLATSVD KGECLGGSTL SLLHDRSFSY TGDSQAQELC LYLTKAASAP YFEVLEKWIY RGII HDPYS EFMVEEHELR KERIQEDYND KYWDQRYTIV QQQIPSFLQK MADKILSTGK YLNVVRECGH DVTCPVAKEI IYTLK ERAY VEQIEKAFNY ASKVLLDFLM EEKELVAHLR SIKRYFLMDQ GDFFVHFMDL AEEELRKPVE DITPPRLEAL LELALR MST ANTDPFKDDL KIDLMPHDLI TQLLRVLAIE TKQEKAMAHA DPTELALSGL EAFSFDYIVK WPLSLIINRK ALTRYQM LF RHMFYCKHVE RQLCSVWISN KTAKQHSLHS AQWFAGAFTL RQRMLNFVQN IQYYMMFEVM EPTWHILEKN LKSASNID D VLGHHTGFLD TCLKDCMLTN PELLKVFSKL MSVCVMFTNC MQKFTQSMKL DGELGGQTLE HSTVLGLPAG AEERARKEL ARKHLAEHAD TVQLVSGFEA TINKFDKNFS AHLLDLLARL SIYSTSDCEH GMASVISRLD FNGFYTERLE RLSAERSQKA TPQVPVLRG PPAPAPRVAV TAQ

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Macromolecule #7: Gamma-tubulin complex component 4

MacromoleculeName: Gamma-tubulin complex component 4 / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 76.179969 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MIHELLLALS GYPGSIFTWN KRSGLQVSQD FPFLHPSETS VLNRLCRLGT DYIRFTEFIE QYTGHVQQQD HHPSQQGQGG LHGIYLRAF CTGLDSVLQP YRQALLDLEQ EFLGDPHLSI SHVNYFLDQF QLLFPSVMVV VEQIKSQKIH GCQILETVYK H SCGGLPPV ...String:
MIHELLLALS GYPGSIFTWN KRSGLQVSQD FPFLHPSETS VLNRLCRLGT DYIRFTEFIE QYTGHVQQQD HHPSQQGQGG LHGIYLRAF CTGLDSVLQP YRQALLDLEQ EFLGDPHLSI SHVNYFLDQF QLLFPSVMVV VEQIKSQKIH GCQILETVYK H SCGGLPPV RSALEKILAV CHGVMYKQLS AWMLHGLLLD QHEEFFIKQG PSSGNVSAQP EEDEEDLGIG GLTGKQLREL QD LRLIEEE NMLAPSLKQF SLRVEILPSY IPVRVAEKIL FVGESVQMFE NQNVNLTRKG SILKNQEDTF AAELHRLKQQ PLF SLVDFE QVVDRIRSTV AEHLWKLMVE ESDLLGQLKI IKDFYLLGRG ELFQAFIDTA QHMLKTPPTA VTEHDVNVAF QQSA HKVLL DDDNLLPLLH LTIEYHGKEH KADATQAREG PSRETSPREA PASGWAALGL SYKVQWPLHI LFTPAVLEKY NVVFK YLLS VRRVQAELQH CWALQMQRKH LKSNQTDAIK WRLRNHMAFL VDNLQYYLQV DVLESQFSQL LHQINSTRDF ESIRLA HDH FLSNLLAQSF ILLKPVFHCL NEILDLCHSF CSLVSQNLGP LDERGAAQLS ILVKGFSRQS SLLFKILSSV RNHQINS DL AQLLLRLDYN KYYTQAGGTL GSFGM

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Macromolecule #8: Gamma-tubulin complex component 5

MacromoleculeName: Gamma-tubulin complex component 5 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 118.467547 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MARHGPPWSR LDAQQERDVR ELVRGVAGLQ DEADPNFQLA LNFAWSNFRF HRFLDVNSHK IEKTIEGIYE KFVIHSDLSK AASWKRLTE EFLNAPLPSI KEIKTDAHYS ILSLLLCLSD SPSNSSYVET PRNKEVEKKD DFDWGKYLME DEEMDIGPYM D TPNWSEES ...String:
MARHGPPWSR LDAQQERDVR ELVRGVAGLQ DEADPNFQLA LNFAWSNFRF HRFLDVNSHK IEKTIEGIYE KFVIHSDLSK AASWKRLTE EFLNAPLPSI KEIKTDAHYS ILSLLLCLSD SPSNSSYVET PRNKEVEKKD DFDWGKYLME DEEMDIGPYM D TPNWSEES EEENDQQPLS REDSGIQVDR TPLEEQDQNR KLDPCISWKD EPDDRSWLEH HVVHQYWTAR PSQFPHSLHL HS NLAAVWD QHLYSSDPLY VPDDRVLVTE TQVIRETLWL LSGVKKLFIF QLIDGKVTVR NNIIVTHLTH SCLRSVLEQI AAY GQVVFR LQEFIDEVMG HSSESMLPGS GSVPKKSTEA PFRTYQAFMW ALYKYFISFK EELAEIEKCI INNDTTITLA IVVD KLAPR LSQLKVLHKV FSTGVAEVPP DTRNVVRASH LLNTLYKAIL EYDNVGEASE QTVSLLFSLW VETVRPYLQT VDEWI VHGH LWDGAREFII QRNKNVPVNH RDFWYATYTL YSVSEKTENE EKMSDNASAS SGSDQGPSSR QHTMVSFLKP VLKQII MAG KSMQLLKNLQ CAESTTCQAG ARDAERKSLY TLFLESVQSR LRHGEDSTPQ VLTEQQATKE NLMKMQSIAE SHLELDD VH DPLLAINFAR MYLEQSDFHE KFAGGDVCVD RSSESVTCQT FELTLRSCLY PHIDKQYLDC CGNLMQTLKK DYRLVEYL Q AMRNFFLMEG GDTMYDFYTS IFDKIREKET WQNVSFLNVQ LQEAVGQRYP EDSSRLSISF ENVDTAKKKL PVHILDGLT LSYKVPWPVD IVISLECQKI YNQVFLLLLQ IKWAKYSLDV LLFGELVSTA EKPRLKEGLI HEQDTVAQFG PQKEPVRQQI HRMFLLRVK LMHFVNSLHN YIMTRILHST GLEFQHQVEE AKDLDQLIKI HYRYLSTIHD RCLLREKVSF VKEAIMKVLN L ALMFADGW QAGLGTWRME SIEKMESDFK NCHMFLVTIL NKAVCRGSFP HLESLALSLM AGMEQS

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Macromolecule #9: GUANOSINE-5'-DIPHOSPHATE

MacromoleculeName: GUANOSINE-5'-DIPHOSPHATE / type: ligand / ID: 9 / Number of copies: 14 / Formula: GDP
Molecular weightTheoretical: 443.201 Da
Chemical component information

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM / Guanosine diphosphate

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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: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 58.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER / Details: Ab initio
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.13 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 105181
FSC plot (resolution estimation)

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