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- EMDB-43481: Density map for free recombinant gamma tubulin ring complex -

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Basic information

Entry
Database: EMDB / ID: EMD-43481
TitleDensity map for free recombinant gamma tubulin ring complex
Map datadensity map for free recombinant gamma tubulin ring complex
Sample
  • Complex: Gamma tubulin ring complex
    • Protein or peptide: Isoform 3 of Gamma-tubulin complex component 2
    • Protein or peptide: Gamma-tubulin complex component 3
    • Protein or peptide: Isoform 2 of Gamma-tubulin complex component 4
    • Protein or peptide: Gamma-tubulin complex component 5
    • Protein or peptide: TUBGCP6 protein
    • Protein or peptide: Mitotic-spindle organizing protein 1
    • Protein or peptide: Actin, cytoplasmic 1
    • Protein or peptide: Tubulin gamma-1 chain
KeywordsComplex / CYTOSOLIC PROTEIN
Function / homology
Function and homology information


microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / microtubule nucleator activity / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / polar microtubule / interphase microtubule organizing center / bBAF complex / gamma-tubulin complex / gamma-tubulin ring complex ...microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / microtubule nucleator activity / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / polar microtubule / interphase microtubule organizing center / bBAF complex / gamma-tubulin complex / gamma-tubulin ring complex / npBAF complex / regulation of transepithelial transport / nBAF complex / mitotic spindle microtubule / brahma complex / meiotic spindle organization / morphogenesis of a polarized epithelium / protein localization to adherens junction / postsynaptic actin cytoskeleton / structural constituent of postsynaptic actin cytoskeleton / Formation of the dystrophin-glycoprotein complex (DGC) / GBAF complex / Formation of annular gap junctions / Tat protein binding / Gap junction degradation / regulation of G0 to G1 transition / Folding of actin by CCT/TriC / Cell-extracellular matrix interactions / dense body / microtubule nucleation / regulation of nucleotide-excision repair / Prefoldin mediated transfer of substrate to CCT/TriC / RSC-type complex / apical protein localization / regulation of double-strand break repair / gamma-tubulin binding / adherens junction assembly / RHOF GTPase cycle / Adherens junctions interactions / non-motile cilium / tight junction / Sensory processing of sound by outer hair cells of the cochlea / Interaction between L1 and Ankyrins / SWI/SNF complex / regulation of mitotic metaphase/anaphase transition / Sensory processing of sound by inner hair cells of the cochlea / positive regulation of T cell differentiation / regulation of norepinephrine uptake / transporter regulator activity / apical junction complex / nitric-oxide synthase binding / positive regulation of double-strand break repair / pericentriolar material / maintenance of blood-brain barrier / NuA4 histone acetyltransferase complex / establishment or maintenance of cell polarity / cortical cytoskeleton / cell leading edge / positive regulation of stem cell population maintenance / Regulation of MITF-M-dependent genes involved in pigmentation / microtubule organizing center / Recycling pathway of L1 / regulation of synaptic vesicle endocytosis / regulation of G1/S transition of mitotic cell cycle / brush border / mitotic sister chromatid segregation / kinesin binding / EPH-ephrin mediated repulsion of cells / negative regulation of cell differentiation / single fertilization / mitotic spindle assembly / RHO GTPases Activate WASPs and WAVEs / positive regulation of myoblast differentiation / RHO GTPases activate IQGAPs / positive regulation of double-strand break repair via homologous recombination / regulation of protein localization to plasma membrane / cytoplasmic microtubule / spindle assembly / cytoplasmic microtubule organization / cytoskeleton organization / EPHB-mediated forward signaling / substantia nigra development / centriole / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / calyx of Held / Recruitment of mitotic centrosome proteins and complexes / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / axonogenesis / AURKA Activation by TPX2 / condensed nuclear chromosome / mitotic spindle organization / meiotic cell cycle / Translocation of SLC2A4 (GLUT4) to the plasma membrane / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / adherens junction / positive regulation of cell differentiation / actin filament / FCGR3A-mediated phagocytosis
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
TUBGCP6 protein / Tubulin gamma-1 chain / Actin, cytoplasmic 1 / Mitotic-spindle organizing protein 1 / Gamma-tubulin complex component 3 / 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: 7.0 Å
AuthorsAher A / Urnavicius L / Kapoor TM
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)GM130234 United States
CitationJournal: Nat Struct Mol Biol / Year: 2024
Title: Structure of the γ-tubulin ring complex-capped microtubule.
Authors: Amol Aher / Linas Urnavicius / Allen Xue / Kasahun Neselu / Tarun M Kapoor /
Abstract: Microtubules are composed of α-tubulin and β-tubulin dimers positioned head-to-tail to form protofilaments that associate laterally in varying numbers. It is not known how cellular microtubules ...Microtubules are composed of α-tubulin and β-tubulin dimers positioned head-to-tail to form protofilaments that associate laterally in varying numbers. It is not known how cellular microtubules assemble with the canonical 13-protofilament architecture, resulting in micrometer-scale α/β-tubulin tracks for intracellular transport that align with, rather than spiral along, the long axis of the filament. We report that the human ~2.3 MDa γ-tubulin ring complex (γ-TuRC), an essential regulator of microtubule formation that contains 14 γ-tubulins, selectively nucleates 13-protofilament microtubules. Cryogenic electron microscopy reconstructions of γ-TuRC-capped microtubule minus ends reveal the extensive intra-domain and inter-domain motions of γ-TuRC subunits that accommodate luminal bridge components and establish lateral and longitudinal interactions between γ-tubulins and α-tubulins. Our structures suggest that γ-TuRC, an inefficient nucleation template owing to its splayed conformation, can transform into a compacted cap at the microtubule minus end and set the lattice architecture of cellular microtubules.
History
DepositionJan 21, 2024-
Header (metadata) releaseMar 27, 2024-
Map releaseMar 27, 2024-
UpdateOct 9, 2024-
Current statusOct 9, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_43481.png

Downloads & links

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Map

FileDownload / File: emd_43481.map.gz / Format: CCP4 / Size: 190.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationdensity map for free recombinant gamma tubulin ring complex
Projections & slices

Image control

Size
Brightness
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.32 Å/pix.
x 368 pix.
= 485.76 Å		1.32 Å/pix.
x 368 pix.
= 485.76 Å		1.32 Å/pix.
x 368 pix.
= 485.76 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.32 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.004
Minimum - Maximum-0.019384384 - 0.051558703
Average (Standard dev.)0.00028123858 (±0.0017953764)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions368368368
Spacing368368368
CellA=B=C: 485.76 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_43481_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map for the free recombinant gamma tubulin ring complex

Fileemd_43481_half_map_1.map
AnnotationHalf map for the free recombinant gamma tubulin ring complex
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map for the density map for free...

Fileemd_43481_half_map_2.map
AnnotationHalf map for the density map for free recombinant gamma tubulin ring complex
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Gamma tubulin ring complex

EntireName: Gamma tubulin ring complex
Components
  • Complex: Gamma tubulin ring complex
    • Protein or peptide: Isoform 3 of Gamma-tubulin complex component 2
    • Protein or peptide: Gamma-tubulin complex component 3
    • Protein or peptide: Isoform 2 of Gamma-tubulin complex component 4
    • Protein or peptide: Gamma-tubulin complex component 5
    • Protein or peptide: TUBGCP6 protein
    • Protein or peptide: Mitotic-spindle organizing protein 1
    • Protein or peptide: Actin, cytoplasmic 1
    • Protein or peptide: Tubulin gamma-1 chain

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Supramolecule #1: Gamma tubulin ring complex

SupramoleculeName: Gamma tubulin ring complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #5, #1, #7-#8, #2-#4, #6
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Gamma-tubulin complex component 3

MacromoleculeName: Gamma-tubulin complex component 3 / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 103.710102 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
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 #2: TUBGCP6 protein

MacromoleculeName: TUBGCP6 protein / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 199.732516 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
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 LERKASKLSA EAARREQKAL WRIQRHRLES ARLRFLLEDE KHIQEMLKA VSEAHQPQEP PDVLLSVHPQ VTSPGPEHPE GGQGCDSGSA EQHSPAWDGW NRPGLLTPQP LKPLAVGAGG RGLQQAEGAR PFSDSLSIG DFLPVGPGAE PSVQTGMVPL LEVALQTINL DLPPSAPGEA PAAASTQPSR PQEYDFSTVL RPAVATSPAP G PLQAAECS LGSSGLQLWE DSCGKMDACG SASRETLLPS HPPRRAALEE GSSQPTERLF GQVSGGGLPT GDYASEIAPT RP RWNTHGH VSDASIRVGE NVSDVAPTQP RWNTHGHVSN ASISLGESVS DVAPTRPRWN IHGHVSNASI RVGENVSDVA PTR PRWNTH GHVSNASIRV GENVSDVAPT RPRWNTHGHV SDASISLGES VSDMAPARPR WNTHGHVSDA SISLGESVSD MAPT RPRWN THGHVSDTSI RVGENVSDVA PIRSRCNTHG HVSDASISLG EPVSDVVSTR PRWNTHVPIP PPHMVLGALS PEAEP NTPR PQQSPPGHTS QSALSLGAQS AVLDCGPRLP VEVGPSLSSP SSGCGEGSIS VGENVSDVAP TQPWWPNTPG DSVSEE LGP GRSGDTEDLS PNWPLNSQED TAAQSSPGRG EEAEASAAEA QGGEQAYLAG LAGQYHLERY PDSYESMSEP PIAHLLR PV LPRAFAFPVD PQVQSAADET AVQLSELLTL PVLMKRSITA PLAAHISLVN KAAVDYFFVE LHLEAHYEAL RHFLLMED G EFAQSLSDLL FEKLGAGQTP GELLNPLVLN SVLSKALQCS LHGDTPHASN LSLALKYLPE VFAPNAPDVL SCLELRYKV DWPLNIVITE GCLSKYSGVF SFLLQLKLMM WALKDVCFHL KRTALLSHMA GSVQFRQLQL FKHEMQHFVK VIQGYIANQI LHVTWCEFR ARLATVGDLE EIQRAHAEYL HEAVFRGLLT EKAAPVMNVI HSIFSLVLKF RSQLISQAWG PPGGPRGAEH P NFALMQQS YNTFKYYSHF LFKVVTKLVN RGYQPHLEDF LLRINFNNYY QDA

UniProtKB: TUBGCP6 protein

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Macromolecule #3: Mitotic-spindle organizing protein 1

MacromoleculeName: Mitotic-spindle organizing protein 1 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.485724 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
MASSSGAGAA AAAAAANLNA VRETMDVLLE ISRILNTGLD METLSICVRL CEQGINPEAL SSVIKELRKA TEALKAAENM TS

UniProtKB: Mitotic-spindle organizing protein 1

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Macromolecule #4: Actin, cytoplasmic 1

MacromoleculeName: Actin, cytoplasmic 1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.78266 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
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 #5: Isoform 3 of Gamma-tubulin complex component 2

MacromoleculeName: Isoform 3 of Gamma-tubulin complex component 2 / type: protein_or_peptide / ID: 5 / Number of copies: 5 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 105.5815 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
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 TDTALPIVLL GWSLALSPRL KCSGVISAHC GLHLPGTLPL AS QESAVVE DLLYVLVGVD GRYVSAQPLA GRQSRTFLVD PNLDLSIREL VHRILPVAAS YSAVTRFIEE KSSFEYGQVN HAL AAAMRT LVKEHLILVS QLEQLHRQGL LSLQKLWFYI QPAMRTMDIL ASLATSVDKG ECLGGSTLSL LHDRSFSYTG DSQA QELCL YLTKAASAPY FEVLEKWIYR GIIHDPYSEF MVEEHELRKE RIQEDYNDKY WDQRYTIVQQ QIPSFLQKMA DKILS TGKY LNVVRECGHD VTCPVAKEII YTLKERAYVE QIEKAFNYAS KVLLDFLMEE KELVAHLRSI KRYFLMDQGD FFVHFM DLA EEELRKPVED ITPPRLEALL ELALRMSTAN TDPFKDDLKI DLMPHDLITQ LLRVLAIETK QEKAMAHADP TELALSG LE AFSFDYIVKW PLSLIINRKA LTRYQMLFRH MFYCKHVERQ LCSVWISNKT AKQHSLHSAQ WFAGAFTLRQ RMLNFVQN I QYYMMFEVME PTWHILEKNL KSASNIDDVL GHHTGFLDTC LKDCMLTNPE LLKVFSKLMS VCVMFTNCMQ KFTQSMKLD GELGGQTLEH STVLGLPAGA EERARKELAR KHLAEHADTV QLVSGFEATI NKFDKNFSAH LLDLLARLSI YSTSDCEHGM ASVISRLDF NGFYTERLER LSAERSQKAT PQVPVLRGPP APAPRVAVTA Q

UniProtKB: Gamma-tubulin complex component 2

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Macromolecule #6: Tubulin gamma-1 chain

MacromoleculeName: Tubulin gamma-1 chain / type: protein_or_peptide / ID: 6 / Number of copies: 14 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 52.022617 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
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 WGTQEQENLY FQ

UniProtKB: Tubulin gamma-1 chain

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Macromolecule #7: Isoform 2 of Gamma-tubulin complex component 4

MacromoleculeName: Isoform 2 of 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: 76.108898 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
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 KDATQAREGP SRETSPREAP ASGWAALGLS YKVQWPLHIL FTPAVLEKYN VVFKY LLSV RRVQAELQHC WALQMQRKHL KSNQTDAIKW RLRNHMAFLV DNLQYYLQVD VLESQFSQLL HQINSTRDFE SIRLAH DHF LSNLLAQSFI LLKPVFHCLN EILDLCHSFC SLVSQNLGPL DERGAAQLSI LVKGFSRQSS LLFKILSSVR NHQINSD LA QLLLRLDYNK YYTQAGGTLG SFGM

UniProtKB: Gamma-tubulin complex component 4

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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: 118.367406 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
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 TPLEEQDQNG 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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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 6.8
VitrificationCryogen name: ETHANE / Chamber humidity: 100 %

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

6v6s

Final reconstructionResolution.type: BY AUTHOR / Resolution: 7.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 98558
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementProtocol: RIGID BODY FIT
Output model

PDB-8vrd:
Rigid body fitted model for free recombinant gamma tubulin ring complex.

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