[English] 日本語
Yorodumi
- EMDB-19861: Vertebrate microtubule-capping gamma-tubulin ring complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-19861
TitleVertebrate microtubule-capping gamma-tubulin ring complex
Map dataCryo-EM reconstruction of the vertebrate microtubule-capping gamma-tubulin ring complex isolated from Xenopus leavis egg extract
Sample
  • Complex: Vertebrate microtubule-capping gamma-tubulin ring complex
    • Protein or peptide: Mitotic-spindle organizing protein 1
    • Protein or peptide: Gamma-tubulin complex component 3 homolog
    • Protein or peptide: Gamma-tubulin complex component
    • Protein or peptide: Gamma-tubulin complex component 6
    • Protein or peptide: Tubulin gamma-1 chain
    • Protein or peptide: Gamma-tubulin complex component
    • Protein or peptide: Gamma-tubulin complex component
Keywordscytoskeleton / microtubule / microtubule nucleation / complex / template / cap / gamma-tubulin / gamma-tubulin ring complex / CELL CYCLE
Function / homology
Function and homology information


gamma-tubulin complex localization / mitotic spindle microtubule / gamma-tubulin ring complex / polar microtubule / gamma-tubulin complex / microtubule nucleation / gamma-tubulin binding / cytoplasmic microtubule organization / spindle / spindle pole ...gamma-tubulin complex localization / mitotic spindle microtubule / gamma-tubulin ring complex / polar microtubule / gamma-tubulin complex / microtubule nucleation / gamma-tubulin binding / cytoplasmic microtubule organization / spindle / spindle pole / microtubule / centrosome / GTP binding / cytoplasm
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 / 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
Similarity search - Domain/homology
Gamma-tubulin complex component / Gamma-tubulin complex component / Gamma-tubulin complex component 6 / Gamma-tubulin complex component 3 homolog / Tubulin gamma-1 chain / Mitotic-spindle organizing protein 1 / Gamma-tubulin complex component
Similarity search - Component
Biological speciesXenopus laevis (African clawed frog)
Methodsingle particle reconstruction / cryo EM / Resolution: 17.0 Å
AuthorsVermeulen BJA / Pfeffer S
Funding support Germany, 6 items
OrganizationGrant numberCountry
German Research Foundation (DFG)PF 963/1-4 Germany
German Research Foundation (DFG)Schi 195/4-4 Germany
Other private
German Research Foundation (DFG)INST 35/1503-1 FUGG Germany
German Research Foundation (DFG)INST 35/1134-1 FUGG Germany
German Research Foundation (DFG)INST 35/1314-1 FUGG Germany
CitationJournal: EMBO J / Year: 2024
Title: γ-TuRC asymmetry induces local protofilament mismatch at the RanGTP-stimulated microtubule minus end.
Authors: Bram Ja Vermeulen / Anna Böhler / Qi Gao / Annett Neuner / Erik Župa / Zhenzhen Chu / Martin Würtz / Ursula Jäkle / Oliver J Gruss / Stefan Pfeffer / Elmar Schiebel /
Abstract: The γ-tubulin ring complex (γ-TuRC) is a structural template for de novo microtubule assembly from α/β-tubulin units. The isolated vertebrate γ-TuRC assumes an asymmetric, open structure ...The γ-tubulin ring complex (γ-TuRC) is a structural template for de novo microtubule assembly from α/β-tubulin units. The isolated vertebrate γ-TuRC assumes an asymmetric, open structure deviating from microtubule geometry, suggesting that γ-TuRC closure may underlie regulation of microtubule nucleation. Here, we isolate native γ-TuRC-capped microtubules from Xenopus laevis egg extract nucleated through the RanGTP-induced pathway for spindle assembly and determine their cryo-EM structure. Intriguingly, the microtubule minus end-bound γ-TuRC is only partially closed and consequently, the emanating microtubule is locally misaligned with the γ-TuRC and asymmetric. In the partially closed conformation of the γ-TuRC, the actin-containing lumenal bridge is locally destabilised, suggesting lumenal bridge modulation in microtubule nucleation. The microtubule-binding protein CAMSAP2 specifically binds the minus end of γ-TuRC-capped microtubules, indicating that the asymmetric minus end structure may underlie recruitment of microtubule-modulating factors for γ-TuRC release. Collectively, we reveal a surprisingly asymmetric microtubule minus end protofilament organisation diverging from the regular microtubule structure, with direct implications for the kinetics and regulation of nucleation and subsequent modulation of microtubules during spindle assembly.
History
DepositionMar 15, 2024-
Header (metadata) releaseApr 17, 2024-
Map releaseApr 17, 2024-
UpdateApr 17, 2024-
Current statusApr 17, 2024Processing site: PDBe / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_19861.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCryo-EM reconstruction of the vertebrate microtubule-capping gamma-tubulin ring complex isolated from Xenopus leavis egg extract
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
2 Å/pix.
x 256 pix.
= 513.024 Å
2 Å/pix.
x 256 pix.
= 513.024 Å
2 Å/pix.
x 256 pix.
= 513.024 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 2.004 Å
Density
Contour LevelBy AUTHOR: 0.0192
Minimum - Maximum-0.0152010415 - 0.0499322
Average (Standard dev.)-0.00013118725 (±0.005534147)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 513.024 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Half map: Half map 2 of the cryo-EM reconstruction of...

Fileemd_19861_half_map_1.map
AnnotationHalf map 2 of the cryo-EM reconstruction of the vertebrate microtubule-capping gamma-tubulin ring complex isolated from Xenopus leavis egg extract
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: Half map 1 of the cryo-EM reconstruction of...

Fileemd_19861_half_map_2.map
AnnotationHalf map 1 of the cryo-EM reconstruction of the vertebrate microtubule-capping gamma-tubulin ring complex isolated from Xenopus leavis egg extract
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : Vertebrate microtubule-capping gamma-tubulin ring complex

EntireName: Vertebrate microtubule-capping gamma-tubulin ring complex
Components
  • Complex: Vertebrate microtubule-capping gamma-tubulin ring complex
    • Protein or peptide: Mitotic-spindle organizing protein 1
    • Protein or peptide: Gamma-tubulin complex component 3 homolog
    • Protein or peptide: Gamma-tubulin complex component
    • Protein or peptide: Gamma-tubulin complex component 6
    • Protein or peptide: Tubulin gamma-1 chain
    • Protein or peptide: Gamma-tubulin complex component
    • Protein or peptide: Gamma-tubulin complex component

-
Supramolecule #1: Vertebrate microtubule-capping gamma-tubulin ring complex

SupramoleculeName: Vertebrate microtubule-capping gamma-tubulin ring complex
type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Details: Vertebrate microtubule-capping gamma-tubulin ring complex induced through the RanGTP spindle assembly pathway and isolated from Xenopus laevis egg extract
Source (natural)Organism: Xenopus laevis (African clawed frog)

-
Macromolecule #1: Mitotic-spindle organizing protein 1

MacromoleculeName: Mitotic-spindle organizing protein 1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 7.749854 KDa
SequenceString:
MANASGNMSA VRETMDVLLE ISRLLNTGLD METLSICVRL CEQGINPEAL SSVIKELRRA SDTLKASEST AS

UniProtKB: Mitotic-spindle organizing protein 1

-
Macromolecule #2: Gamma-tubulin complex component 3 homolog

MacromoleculeName: Gamma-tubulin complex component 3 homolog / type: protein_or_peptide / ID: 2 / Number of copies: 5 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 103.789352 KDa
SequenceString: MAVPDQKSPN VLLQNLCCRI LGKGEADVAQ QFQYAVRVIG SNFAPTVERD EFLVTEKIKK EFVRQRREAD GALFSELHRK LQSQGVLKN RWSILYLLLS LSEDPRKQPN KTSSFAALFA QALPRDAHST PYYYARPQSL PLSYQDRNVQ CAQNAASIGS S GISSIGMY ...String:
MAVPDQKSPN VLLQNLCCRI LGKGEADVAQ QFQYAVRVIG SNFAPTVERD EFLVTEKIKK EFVRQRREAD GALFSELHRK LQSQGVLKN RWSILYLLLS LSEDPRKQPN KTSSFAALFA QALPRDAHST PYYYARPQSL PLSYQDRNVQ CAQNAASIGS S GISSIGMY ALNGPTPQSI IQGQSNQTPN MGDALRQQLG SRLAWTLAAG QQPSQQSTTT KGLPNTVSRN VPRTRREGDS SG SVEITET SLVRDLLYVF QGIDGKFVKM CNSENCYKVD GKVAVSKSLK DITSKLSELG WLHNKIKKYT DQRSLDRAFG LVG QSFCAA LHQELKEYYR LLSVLHSQLQ VEDDQGVNLG VESSLTLRRL LVWTFDPKIR LKTLAALVDH CQGRKGGELA SAVH AYTKT GDPYMRSLVQ HILGLVAYPI LNFLYRWIYD GELEDTYHEF FVASDPVVKT DRLWHDKYSL RKSMIPSFMT MDQSR KVLL IGKSINFLHQ VCHDQTPASK AMAVGKSAES PKDAAELFTD LENAFQTKID AAYFDTSKYL LDVLNKNYNL LEHMQA MRR YLLLGQGDFI RHLMDLLKPE LVRPATTLYQ HNLTGILETA VRATNAQFDN PEILKRLDVR LLEVSPGDTG WDVFSLD YH VDGPIATVFT RECMSHYLRV FNFLWRAKRM EYILTDIWKG HMCNAKLLKG MPELSGVLHQ CHILASEMVH FIHQMQYY I TFEVLECSWD ELWNKVLKAQ DLDHIIAAHD VFLDTIISRC LLDSESRALL NQLRAVFDQI IEFQNAQDAL YRAALEELQ QRLQFEERKK ERESEGEWGV TAAEEDVENK RIQEFQESIP KMRSQLRILT HFYQGIVQQF LVLLTTSTDE SLRFLSFRLD FNEHYKARE PRLRVSMGTR GRRSFHV

UniProtKB: Gamma-tubulin complex component 3 homolog

-
Macromolecule #3: Gamma-tubulin complex component

MacromoleculeName: Gamma-tubulin complex component / type: protein_or_peptide / ID: 3 / Number of copies: 5 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 103.468312 KDa
SequenceString: MSEFRIHHDV NELISLLHVF GLEGADVYID LLQKNRTPYV TTSVSTHSAK VKIAEFSRTP DDFLKKYEEL KSKNTRNLDP LVYLLSKLI EDKETLQYLQ QNAKDKAELA TSSVTSVSLP IAPNTSKISM QELEELRRQL ETATVAVSCS HQPVEVLRKF L RDKLNKKH ...String:
MSEFRIHHDV NELISLLHVF GLEGADVYID LLQKNRTPYV TTSVSTHSAK VKIAEFSRTP DDFLKKYEEL KSKNTRNLDP LVYLLSKLI EDKETLQYLQ QNAKDKAELA TSSVTSVSLP IAPNTSKISM QELEELRRQL ETATVAVSCS HQPVEVLRKF L RDKLNKKH TGHPVPVFPS WVYERPALTG DFMSFSNPST DVTVSIGTLP LPSQETCLVE DLLYILIGVD GRYISVQPLV GR QSRSFSV EQNLDSSVKE LVNRILPVAT NYSTVTRFVE ENSSFEYGQV NHALGAAMRT LGKEYMILIS QLEHLQRQGL LSL QKLWFY IQPTLRTMEV LASIATSLNK GECFGGATLS LLHDRTFGYT GDSQAQELCL YLTKAASAPY FDILERWIYR GIIN DPYSE FMVEEHELQK EKIQEDYNDK YWDQRYTIVQ QQIPSFLQKV ADKILSTGKY LNVVRECGHD VTCPDAKEIT YTLKE QAYV ERIEKAYNYA SKVLLDFLME EEELVAHLRS IKHYFLMDQG DFFVHFMDLT EEELKKPVDD IIPTRLEALL ELALRM STA NTDPFKDDLK IELMPHDLIT QLLRVLAIET HQEKALINSD PTELALSGLE SFSFDYIVKW PLSLIINRKA LTRYQML FR HMFYCKHVER LLCNVWISNK TAKQFSLHSA KWFAGAFTLR QRMLNFVQNI QYYMMFEVME PTWHILEKNL KSASNIDD V LSHHTSFLDN CLKDCMLTNP ELLKIFSKLM SVCVMFTNCL QRFTQSMQVQ TEMEHLTLEH GTMMGPPTQC ERTEEALKK KLTSKYLEEH IDKFPSSFGF ESTINNFDSN FSAHLMDLLD KLSMYSTSDC EHSMINIIYR LDFNGFYTER LKQLSSERNQ KSAPLLGPA QHAVSTK

UniProtKB: Gamma-tubulin complex component

-
Macromolecule #4: Gamma-tubulin complex component 6

MacromoleculeName: Gamma-tubulin complex component 6 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 193.069141 KDa
SequenceString: MDSITKLFGD LCESHMVGFP WRTALNSRKH SKNRTKQTLK KLAYDTLFVH LFQDEARKLQ PNCTRLPVKN KIIMLSFNLR ICGMSSEAD RLEELVEYLE QSNGIQISDL HAVLELLVEL SGTGPPQLLP PKRDYFKNNK YVGRNVKYQG YDYYDVQVFE A DLGTTVAY ...String:
MDSITKLFGD LCESHMVGFP WRTALNSRKH SKNRTKQTLK KLAYDTLFVH LFQDEARKLQ PNCTRLPVKN KIIMLSFNLR ICGMSSEAD RLEELVEYLE QSNGIQISDL HAVLELLVEL SGTGPPQLLP PKRDYFKNNK YVGRNVKYQG YDYYDVQVFE A DLGTTVAY QELEISTTIQ RTLQIMEAAP GTGLPALSFF SQNDLSTDKF EKETRGSLFG ALVHSRTNDM DIKLDMPPVP EN ADLSGLA IKVPQSIDQS EDEGFQSASN MTPDSQSEPS MTPDIDVWEA VLTYGPSKRR CWERIGCPPG KREEPYVTEA GRE AFDKLY KLHEGGLQIL SATTLQPQLV LLEETDLVKA VLNVLIGVVS STFSYNQALQ SFAVKQGVYI SGTSPDNVSS LLTQ VAEYG TYYTRLSHFS LLTVLDSSHS NGLVFQAFTS GLRKYLQYYR ACVLSTPASL TLLTISFLFR KLGRQLRYLA ELCCI GTLV TSATRGISTA FPTGVKLLSY LYKEALENSS NENYPVLLSL LKTSCEPYTR FIYDWVYSGV FRDVCGEFMI QVNEDY LGF RDKRYWTHGY VLISKEVEDC VPVFLKHVAN EIYICGKTIN LLKLCCPKHY ICWSDIPVPR ISVTFSLEEL KEMEKDC AV YVARMERIAR HSCISKEQKA LQTEIARQEL IIQARETTEK VFETFKDRKL AEKLSLDTKK RELFQKLKDQ YEKEQERR L TTKQEEADDD FSYAREIRDR EKRLKALEEE LELKTRQELI EHYSRLSEEA TRKEQRALWK LQRHKLETIR LKFFLEEQK RMQDLVANFP VDICEENLGV LPDGEISHQT DNTNDAGLGN IENEKSVPEQ HALHNNNDEV YTAQNCISKS ESLCVDVTLP TENVHSQTS NASVLGVPSF DSNLCTPDVD IIDFLPTLPS ENQEVAVVQS LVDDALISIG SDLNTDTKDK ESLCALKSDL Q ESSTGSEY DFKTILKPIA CTQVSQGHIK IGEYSSNVQP ARPRWSTHGH SSDSNIKIGN YVSDINVHQP KHSQHGHSSD SN INISDHM SDVEPRLPRL NLHGHISTGH IKVGEYASDV EPSTPRHSVH GHASQGNIKI GENVSDVKLS RPRWNIHGHV SDA NIKIGE NTSEIAPLRP RWNIHGHASQ SHIKIGELVS DIEPSQPRRT PFGHPSQSSI PIGDQPVEKY AQKSESEVHS SNST IQHLL YSNIPDKNKD TGGTLTDSPV PVPDQGNSND DTEKRSSTLE QRVQAADSVC DGEASPNTAQ SLPCMSDTLD FGTNG EENV GNDDHTWEKQ QEYLKGLAEK YCLEKYQDSY ELMSHPPVLH LYSNVMPNRF SFPTDSDIKS ATDETTVQLI ELLSLP VLM KYSVTAPMVS HVYLVNKAIV DYYFVELKME RHFEAMRHFL LMEDGEFAQS LSDMLFEKLG SGQTPSELLN PLVLNSI LN KALQYSLHGD SSLASNLTFA LKYLPEVFTP TAPDALSCLE LKYKVDWPLN IVITDTCMNK YSRIFSFLLQ LKHMVWTL R DVWFHLKRTA LVNQASNSVQ YRQLQLYRHE MQHFVKVIQG YIANQILHVT WCEFRNKLSA VSNLEEIYKT HADYLNKAL FRGLLTEKAA PLMNIIHSIF SLILKFRLQL ISQSWICDTG KQMAVHPNFG LMQQSYNTFK YYSDFLFEVV SKLVNRGYQP HLEDFLLRI NFNSYYKQS

UniProtKB: Gamma-tubulin complex component 6

-
Macromolecule #5: Tubulin gamma-1 chain

MacromoleculeName: Tubulin gamma-1 chain / type: protein_or_peptide / ID: 5 / Number of copies: 14 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 51.226719 KDa
SequenceString: MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY IPRAVLLDLE PRVIHSILNS PYANLYNPE NIYLSEHGGG AGNNWASGFS QGEKIHEDIF DIIDREADGS DSLEGFVLCH SIAGGTGSGL GSYLLERLND R YPKKLVQT ...String:
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY IPRAVLLDLE PRVIHSILNS PYANLYNPE NIYLSEHGGG AGNNWASGFS QGEKIHEDIF DIIDREADGS DSLEGFVLCH SIAGGTGSGL GSYLLERLND R YPKKLVQT YSVFPNQDEM SHVVVQPYNS LLTLKRLTQN ADCVVVLDNT ALNRIATDRL HIQNPSFSQI NQLVSTIMSA ST TTLRYPG YMNNDLIGLI ASLIPTPRLH FLMTGYTPLT TDQSVASVRK TTVLDVMRRL LQPKNVMVST GRDRQTNHCY IAI LNIIQG EVDPTQVHKS LQRIRERKLA NFIPWGPASI QVALSRKSPY LPSAHRVSGL MMANHTNISS LFERTCRQYD KLRK REAFL EQFRKEDIFK DNFDELDNSR EIVQQLIDEY HAATRPDYIS WGTQDK

UniProtKB: Tubulin gamma-1 chain

-
Macromolecule #6: Gamma-tubulin complex component

MacromoleculeName: Gamma-tubulin complex component / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 117.577633 KDa
SequenceString: MAHWTRFERD QEGDIKKLVS LMSGIQDDQD GNFQQALQFA WSNFRFHRYL DVSSHTVLRT LEGIFEKLVV HSDLEKAESW KRLTEEFLL LPLPNTEGTK TDSHFAVLSL LLCLSDSPSN HDYTEKPRKK ENDEQEPFDW GKYLREGEDI EFSPDADTPE W SEASEEED ...String:
MAHWTRFERD QEGDIKKLVS LMSGIQDDQD GNFQQALQFA WSNFRFHRYL DVSSHTVLRT LEGIFEKLVV HSDLEKAESW KRLTEEFLL LPLPNTEGTK TDSHFAVLSL LLCLSDSPSN HDYTEKPRKK ENDEQEPFDW GKYLREGEDI EFSPDADTPE W SEASEEED AQEPPSREDS GIQVDRTPLE DPEKKGAPPL VSWKVGEPDA RSWLEQHIVH QYWTSRAPRF SHSSHLHSNL SA IWDQHLY TTDPLYTPDD KTIVTETQVI RETLWLLSGV KKLLIFQLND GKVNVRNDII VTHMTQNCLR SVLEQIAAYG QVV FRLQKF IDEITGHGSE VPLPGTLPTA KKTTEAPFRT YQAFMWALYK YFISFKEELT EIEKCIINKD ETVTLAIVLD KLAP RLAQL KVLHRVFSTG IAEVPPDTRN VVRASHLLNT LYKAILDYDN VGEASEQTVS LLFCLWVETV RPYLEIVDEW IVHGN LFDP AKEFIIQRNK DVPFNHRDFW YATYTLYSVS EKTENEDKMS DNASASSGSD QAPAGRQHTM VSFLKPVLKQ IIMAGK SMQ LLKNLKCRTA LQQDSSRDSD RKSLYTLFLE SVQSRLQHGN DSVPDIITEQ QVNKLSLIKM QSIVAKHLEL DEVHDPL LA INFVRLYLEQ SDFLETFTCN EVCVDRSSES VTCQSFELTL RSCLYPHIGK QYLECCGNLM YTLKKDYRLV EYLQAMRN F FLLEAGDTMY DFYTPIFDKI REKEPWLNLS YLNVQIQEAV GQRYPDDSTR LSVSFESVDL AKKKLPVHTL DGLILSYKV PWPVDIVISS ECQKIYNQVF LLLLLIKWAK YSLDVLQFNE LGNASENEST KEGATVEPFP LPPLTSPSEP KGQQIHRMFL LRVKLMHFV NSLHNYLMTR ILHSTGLEFQ HQVEEAKDLD QLIKIHYRYL STIHDRCLLR EKVSSVKEAI MKVLNVVLMF A DRWHAGLG AWKKESIVKM ESDFTNCHKF LVKVLNKAVC RGSFPHLESL ALSLMAGMEQ S

UniProtKB: Gamma-tubulin complex component

-
Macromolecule #7: Gamma-tubulin complex component

MacromoleculeName: Gamma-tubulin complex component / type: protein_or_peptide / ID: 7 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 76.122961 KDa
SequenceString: MIHELLLALS GYPGSIFTWN KRTGLQVSQD IPFLHPGETS VLNRLCKLGT DYIRFTEFIE QYTGHVQQQD HHPSQQGQVG LHGIYLRAF CRGLDSILQP YRQALLDLEQ EFLADPHLSI SHINYSLDQF HLLFPSIMVV VEQIKSQKIH GCQILETVYK H SCGGLPPV ...String:
MIHELLLALS GYPGSIFTWN KRTGLQVSQD IPFLHPGETS VLNRLCKLGT DYIRFTEFIE QYTGHVQQQD HHPSQQGQVG LHGIYLRAF CRGLDSILQP YRQALLDLEQ EFLADPHLSI SHINYSLDQF HLLFPSIMVV VEQIKSQKIH GCQILETVYK H SCGGLPPV RSALEKTLAV CHGVMYKQLS AWMLHGLLLD QYEEFFVRQG SSSGNLAAAF EEEEDDLGIG GLTGKQLREL QD LRLIEEE NMLAPSLKQF SLRAEMLPSY IPVRVAEKIL FVGESVQMFE NQNVNMSRTG SILKNQEDTF AAELHRLKQQ PLF SLVDFE SVLDRIRSTV AEHLWKLMVE ESDLLGQLKI IKDFYLLGRG ELFQAFIDVA QNMLKTPPTA VTEHDVNVAF QLSA HKVLL DDDNLLPLLN LTIDYHGKEH KDTSQPREGP FRDMSPREAP TSGWAALGLS YKVQWPLHIL FTPAVLEKYN VVFKY LLSV RRVQSELQHC WALQMQRKHL ESNKTDAIKW RLQNHMAFLV DNLQYYLQVD VLESQFSQLL QQINSTRDFE SIRLAH DHF LSNLLAQSFI LLKPVFHCLN EILELCHSFC SLVSQNLGPL DERGAGQLDI LVKGFSCQSS LLFRILSSVR NHQINPD LA QLLLRLDYNK YYTQAGGTLG SFGL

UniProtKB: Gamma-tubulin complex component

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 6.8
GridModel: Quantifoil R2/1 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 295 K / Instrument: FEI VITROBOT MARK IV

-
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 / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 33000
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 BIOQUANTUM (6k x 4k) / Average electron dose: 43.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: EMDB MAP
EMDB ID:

Details: GRIP2 and gamma-tubulin in spokes 5 and 6 were removed
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.1)
Final reconstructionResolution.type: BY AUTHOR / Resolution: 17.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Number images used: 8497

-
Atomic model buiding 1

Initial model
PDB IDChain

source_name: PDB, initial_model_type: experimental model
source_name: AlphaFold, initial_model_type: in silico model
RefinementProtocol: RIGID BODY FIT
Output model

PDB-9eoj:
Vertebrate microtubule-capping gamma-tubulin ring complex

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more