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- EMDB-14013: Structure of recombinant human gamma-Tubulin Ring Complex 12-spok... -

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Basic information

Entry
Database: EMDB / ID: EMD-14013
TitleStructure of recombinant human gamma-Tubulin Ring Complex 12-spoked assembly intermediate (spokes 3-14, substoichiometric spokes 1-2)
Map data12-spoked assembly intermediate of the gamma-Tubulin Ring Complex (spokes 3-14, substoichiometric 1-2)
Sample
  • Complex: Recombinant human Gamma-Tubulin Ring Complex
    • Protein or peptide: Gamma-tubulin complex component 5
    • Protein or peptide: Tubulin gamma-1 chain
    • Protein or peptide: actin, cytoplasmic 1
    • Protein or peptide: Mitotic-spindle organizing protein 1
    • Protein or peptide: Gamma-tubulin complex component 3
    • Protein or peptide: Gamma-tubulin complex component 2
    • Protein or peptide: Gamma-tubulin complex component 4
    • Protein or peptide: Gamma-tubulin complex component 6
  • Ligand: water
KeywordsAssembly / Intermediate / Complex / CYTOSOLIC PROTEIN
Function / homology
Function and homology information


microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / microtubule nucleator activity / polar microtubule / interphase microtubule organizing center / gamma-tubulin complex / gamma-tubulin ring complex / mitotic spindle microtubule / meiotic spindle organization / microtubule nucleation ...microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / microtubule nucleator activity / polar microtubule / interphase microtubule organizing center / gamma-tubulin complex / gamma-tubulin ring complex / mitotic spindle microtubule / meiotic spindle organization / microtubule nucleation / gamma-tubulin binding / non-motile cilium / pericentriolar material / cell leading edge / microtubule organizing center / mitotic sister chromatid segregation / mitotic spindle assembly / single fertilization / spindle assembly / cytoplasmic microtubule / cytoplasmic microtubule organization / centriole / 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 / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / condensed nuclear chromosome / mitotic spindle organization / meiotic cell cycle / brain development / recycling endosome / structural constituent of cytoskeleton / microtubule cytoskeleton organization / spindle / neuron migration / apical part of cell / spindle pole / Regulation of PLK1 Activity at G2/M Transition / mitotic cell cycle / microtubule cytoskeleton / protein-containing complex assembly / microtubule binding / microtubule / neuron projection / cilium / ciliary basal body / centrosome / GTP binding / structural molecule activity / nucleoplasm / identical protein binding / nucleus / membrane / cytoplasm / cytosol
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. / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Actin / Actin family / Actin / 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
Actin, cytoplasmic 1 / Tubulin gamma-1 chain / 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: 8.7 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: Modular assembly of the principal microtubule nucleator γ-TuRC.
Authors: Martin Würtz / Erik Zupa / Enrico S Atorino / Annett Neuner / Anna Böhler / Ariani S Rahadian / Bram J A Vermeulen / Giulia Tonon / Sebastian Eustermann / Elmar Schiebel / Stefan Pfeffer /
Abstract: The gamma-tubulin ring complex (γ-TuRC) is the principal microtubule nucleation template in vertebrates. Recent cryo-EM reconstructions visualized the intricate quaternary structure of the γ-TuRC, ...The gamma-tubulin ring complex (γ-TuRC) is the principal microtubule nucleation template in vertebrates. Recent cryo-EM reconstructions visualized the intricate quaternary structure of the γ-TuRC, containing more than thirty subunits, raising fundamental questions about γ-TuRC assembly and the role of actin as an integral part of the complex. Here, we reveal the structural mechanism underlying modular γ-TuRC assembly and identify a functional role of actin in microtubule nucleation. During γ-TuRC assembly, a GCP6-stabilized core comprising GCP2-3-4-5-4-6 is expanded by stepwise recruitment, selective stabilization and conformational locking of four pre-formed GCP2-GCP3 units. Formation of the lumenal bridge specifies incorporation of the terminal GCP2-GCP3 unit and thereby leads to closure of the γ-TuRC ring in a left-handed spiral configuration. Actin incorporation into the complex is not relevant for γ-TuRC assembly and structural integrity, but determines γ-TuRC geometry and is required for efficient microtubule nucleation and mitotic chromosome alignment in vivo.
History
DepositionDec 16, 2021-
Header (metadata) releaseJan 26, 2022-
Map releaseJan 26, 2022-
UpdateJul 17, 2024-
Current statusJul 17, 2024Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.0357
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.0357
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7qj8
  • Surface level: 0.0357
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_14013.png

Downloads & links

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Map

FileDownload / File: emd_14013.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotation12-spoked assembly intermediate of the gamma-Tubulin Ring Complex (spokes 3-14, substoichiometric 1-2)
Projections & slices

Image control

Size
Brightness
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
2.66 Å/pix.
x 200 pix.
= 532. Å		2.66 Å/pix.
x 200 pix.
= 532. Å		2.66 Å/pix.
x 200 pix.
= 532. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 2.66 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0357 / Movie #1: 0.0357
Minimum - Maximum-0.0131527465 - 0.16031942
Average (Standard dev.)0.002138463 (±0.009159838)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions200200200
Spacing200200200
CellA=B=C: 532.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z2.662.662.66
M x/y/z200200200
origin x/y/z0.0000.0000.000
length x/y/z532.000532.000532.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS200200200
D min/max/mean-0.0130.1600.002

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Supplemental data

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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: Gamma-tubulin complex component 5
    • Protein or peptide: Tubulin gamma-1 chain
    • Protein or peptide: actin, cytoplasmic 1
    • Protein or peptide: Mitotic-spindle organizing protein 1
    • Protein or peptide: Gamma-tubulin complex component 3
    • Protein or peptide: Gamma-tubulin complex component 2
    • Protein or peptide: Gamma-tubulin complex component 4
    • Protein or peptide: Gamma-tubulin complex component 6
  • Ligand: water

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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)
Molecular weightTheoretical: 2.0 MDa

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Macromolecule #1: Gamma-tubulin complex component 5

MacromoleculeName: Gamma-tubulin complex component 5 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 118.467547 KDa
Recombinant expressionOrganism: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)
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

UniProtKB: Gamma-tubulin complex component 5

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Macromolecule #2: Tubulin gamma-1 chain

MacromoleculeName: Tubulin gamma-1 chain / type: protein_or_peptide / ID: 2 / Number of copies: 12 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 51.22777 KDa
Recombinant expressionOrganism: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)
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 WGTQEQ

UniProtKB: Tubulin gamma-1 chain

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Macromolecule #3: actin, cytoplasmic 1

MacromoleculeName: actin, cytoplasmic 1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.78266 KDa
Recombinant expressionOrganism: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)
SequenceString: MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG ...String:
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG YALPHAILRL DLAGRDLTDY LMKILTERGY SFTTTAEREI VRDIKEKLCY VALDFEQEMA TAASSSSLEK SY ELPDGQV ITIGNERFRC PEALFQPSFL GMESCGIHET TFNSIMKCDV DIRKDLYANT VLSGGTTMYP GIADRMQKEI TAL APSTMK IKIIAPPERK YSVWIGGSIL ASLSTFQQMW ISKQEYDESG PSIVHRKCF

UniProtKB: Actin, cytoplasmic 1

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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: 5 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.485724 KDa
Recombinant expressionOrganism: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)
SequenceString:
MASSSGAGAA AAAAAANLNA VRETMDVLLE ISRILNTGLD METLSICVRL CEQGINPEAL SSVIKELRKA TEALKAAENM TS

UniProtKB: Mitotic-spindle organizing protein 1

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Macromolecule #5: Gamma-tubulin complex component 3

MacromoleculeName: Gamma-tubulin complex component 3 / type: protein_or_peptide / ID: 5 / Number of copies: 7 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 103.710102 KDa
Recombinant expressionOrganism: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)
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

UniProtKB: Gamma-tubulin complex component 3

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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: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 102.666953 KDa
Recombinant expressionOrganism: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)
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

UniProtKB: Gamma-tubulin complex component 2

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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 aff. frugiperda 1 BOLD-2017 (butterflies/moths)
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

UniProtKB: Gamma-tubulin complex component 4

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Macromolecule #8: Gamma-tubulin complex component 6

MacromoleculeName: Gamma-tubulin complex component 6 / type: protein_or_peptide / ID: 8 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 200.733641 KDa
Recombinant expressionOrganism: Spodoptera aff. frugiperda 1 BOLD-2017 (butterflies/moths)
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

UniProtKB: Gamma-tubulin complex component 6

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Macromolecule #9: water

MacromoleculeName: water / type: ligand / ID: 9 / Number of copies: 6 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

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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
GridModel: Quantifoil R2/1 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: OTHER
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 6127 / Average electron dose: 35.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 2.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 436887
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 8.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0) / Number images used: 5443
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0)
Final 3D classificationNumber classes: 1 / Software - Name: RELION (ver. 3.1)

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Atomic model buiding 1

Initial model
PDB IDChain

7as4

chain_id: A, source_name: PDB, initial_model_type: experimental model

7as4

chain_id: B, source_name: PDB, initial_model_type: experimental model

7as4

chain_id: K, source_name: PDB, initial_model_type: experimental model

7as4

chain_id: O, source_name: PDB, initial_model_type: experimental model

7as4

chain_id: 7, source_name: PDB, initial_model_type: experimental model

6v6s

chain_id: J, source_name: PDB, initial_model_type: experimental model

6v6s

chain_id: L, source_name: PDB, initial_model_type: experimental model

6l81

source_name: PDB, initial_model_type: experimental model

6x0u

source_name: PDB, initial_model_type: experimental model
RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-7qj8:
Structure of recombinant human gamma-Tubulin Ring Complex 12-spoked assembly intermediate (spokes 3-14, substoichiometric spokes 1-2)

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