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- EMDB-52362: Structure of the double bead region of bovine collagen VI microfi... -
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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Structure of the double bead region of bovine collagen VI microfibrils. | |||||||||
![]() | EM map of collagen VI bovine microfibril bead region | |||||||||
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![]() | Collagen VI / Col6A1 / Col6A2 / Col6A3 / triple-helix / bovine / microfibril / ECM / extracellular / matrix / fibril / STRUCTURAL PROTEIN / PROTEIN FIBRIL | |||||||||
Function / homology | ![]() Collagen chain trimerization / Collagen biosynthesis and modifying enzymes / Signaling by PDGF / Assembly of collagen fibrils and other multimeric structures / Integrin cell surface interactions / ECM proteoglycans / Collagen degradation / collagen trimer / response to UV / collagen binding ...Collagen chain trimerization / Collagen biosynthesis and modifying enzymes / Signaling by PDGF / Assembly of collagen fibrils and other multimeric structures / Integrin cell surface interactions / ECM proteoglycans / Collagen degradation / collagen trimer / response to UV / collagen binding / extracellular matrix / phosphatidylinositol 3-kinase/protein kinase B signal transduction / serine-type endopeptidase inhibitor activity / sarcolemma / : / neuron apoptotic process / cell adhesion / protein-containing complex / extracellular space / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 12.3 Å | |||||||||
![]() | Godwin ARF / Baldock C / Snee MM / Roseman AM | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Collagen VI microfibril structure reveals mechanism for molecular assembly and clustering of inherited pathogenic mutations Authors: Godwin A / Snee M / Becker M / Dajani R / Collins R / Roseman A / Baldock C | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 482.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 24.1 KB 24.1 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 17.1 KB | Display | ![]() |
Images | ![]() | 22.1 KB | ||
Masks | ![]() | 512 MB | ![]() | |
Filedesc metadata | ![]() | 8.4 KB | ||
Others | ![]() ![]() | 474.5 MB 474.4 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1019.6 KB | Display | ![]() |
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Full document | ![]() | 1019.2 KB | Display | |
Data in XML | ![]() | 25.2 KB | Display | |
Data in CIF | ![]() | 33.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9gtuC ![]() 9hanC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | EM map of collagen VI bovine microfibril bead region | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.943 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Half map: Half map of collagen VI bovine microfibril bead region
File | emd_52362_half_map_1.map | ||||||||||||
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Annotation | Half map of collagen VI bovine microfibril bead region | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map of collagen VI bovine microfibril bead region
File | emd_52362_half_map_2.map | ||||||||||||
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Annotation | Half map of collagen VI bovine microfibril bead region | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Collagen VI microfibrils formed from heterotrimers of col6a1, col...
Entire | Name: Collagen VI microfibrils formed from heterotrimers of col6a1, col6a2 and col6a3 |
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Components |
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-Supramolecule #1: Collagen VI microfibrils formed from heterotrimers of col6a1, col...
Supramolecule | Name: Collagen VI microfibrils formed from heterotrimers of col6a1, col6a2 and col6a3 type: tissue / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Col6a1
Macromolecule | Name: Col6a1 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: MRLPRALLPL LLQACWASAQ DDPVASRAIA FQDCPVDLFF VLDTSESVAL RLKPYGALVD KVKSFTKRF IDNLNDRYYR CDRNLVWNAG ALHYSDEVEI IRGLTRMPSG RDELKSSVDA V KYFGKGTY TDCAIKKGLE ELLVGGSHLK ENKYLVVVTD GHPLEGYKEP ...String: MRLPRALLPL LLQACWASAQ DDPVASRAIA FQDCPVDLFF VLDTSESVAL RLKPYGALVD KVKSFTKRF IDNLNDRYYR CDRNLVWNAG ALHYSDEVEI IRGLTRMPSG RDELKSSVDA V KYFGKGTY TDCAIKKGLE ELLVGGSHLK ENKYLVVVTD GHPLEGYKEP CGGLEDAVNE AK HLGIKVF SVAITPDHLE PRLSIIATDH TYRRNFTAAD WGQSRDAEEV ISQTIDTITD MIK NNVEQV CCSFECQPAR GPPGPRGDPG YEGERGKPGL PGEKGEAGDP GRPGDLGPVG YQGM KGEKG SRGEKGSRGP KGYKGEKGKR GMDGVDGMKG ETGFPGLPGC KGSPGFDGIQ GPPGP KGDP GAFGLKGQKG EPGADGEPGR PGSTGPPGDE GEPGEPGPPG EKGEAGDEGN AGPDGA PGE RGGPGERGPR GTPGARGPRG DPGEAGPQGD QGREGPVGVP GDPGEAGPIG PKGYRGD EG PPGTEGPKGA PGPAGPPGDP GLMGERGEDG PPGNGTEGFP GFPGYPGSRG PPGINGTK G YPGLKGDEGE AGDPGEDNND IAARGAKGAK GYRGPEGPQG PPGHVGPPGP DECEILDII MKMCSCCECK CGPIDILFVL DSSESIGLQN FEIAKDFIVK VIDRLSKDEL VKFEPGQSHA GVVQYSHNQ MQEHVDLRDP NIRNAQDLKE AIKKLQWMGG GTFTGEALQY TRSRLLPPTP N NRIALVIT DGRSDTQRDT TPLSVLCGPD IQVVSVGIKD VFGLAAGSDQ LNVISCQGLA PQ GRPGISL VKENYAELLD DGFLKNITAQ ICIDKKCPDY SCPITFSSPA DITILLDGSA SVG SHNFDI TKRFAKRLAE RFLTASRTDP GQDVRVAVVQ YSGTGQQRPE RAALQFLQNY TVLA NTVDS MDFFNDATDV MDALGYVTRF YREASSNAAK KRLLLFSDGN SQGATPAAIE KAVQE AQRA GVEIFAVVVG RQVNEPHVRV LVTGKAAEYD VVFGERHLFR VPSYQALLRG VFYQTV SRK VALD UniProtKB: Collagen alpha-1(VI) chain |
-Macromolecule #2: Col6a2
Macromolecule | Name: Col6a2 / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: MLRRKGAAKM LRSPCSALLL WGLLGAVHAQ QQEVISPGPS DRNSCPEKAD CPVHVYFVLD TSESITMQS PTDSLLYHMQ QFVLQFISQL QDELYLDQVA LSWRYGGLHF SDLVEVFSPP G SDRASFTK SLQSISSFRR GTFTDCMLAN MTQEVRRHVG KGVVNFAVVI ...String: MLRRKGAAKM LRSPCSALLL WGLLGAVHAQ QQEVISPGPS DRNSCPEKAD CPVHVYFVLD TSESITMQS PTDSLLYHMQ QFVLQFISQL QDELYLDQVA LSWRYGGLHF SDLVEVFSPP G SDRASFTK SLQSISSFRR GTFTDCMLAN MTQEVRRHVG KGVVNFAVVI TDGHVTGSPC GG IKLQAER AREEGIRLFA VPPNLKLNEQ GLRDIANTPH ELYRNNYATM RPDSTEIDQD TIN RIIKVM KHEAYGECYK VSCLEIPGPP GPKGYRGQKG AKGNMGEPGE PGQKGRQGDP GIEG PIGFP GPKGVPGFKG EKGEFGADGR KGAPGLAGKN GTDGQKGKLG RIGPPGCKGD TGDRG PDGY VGEAGSPGER GDQGSKGDPG RPGRRGPPGE NGAKGSKGYQ GNNGAPGSPG LKGAKG GPG PRGPKGEPGR RGDPGTKGGP GSDGPKGEKG DPGPEGPRGL AGEVGNKGAK ANRGLPG PR GPQGTVGEPG KQGSRGDPGD AGPRGDSGQP GPKGDPGRPG FSYPGPRGAP GDKGEPGP P GPEGGRGDFG SKGEPGRKGQ KGEPADPGPP GEPGPRGQRG APGPEGEPGP PGDPGLTEC DVMTYVRETC GCCDCEKRCG ALDVVFVIDS SESIGYTNFT LEKNFVINVV NRLGAIAKDP KSETGTRVG VVQYSHEGTF EAIQLDDERI DSLSSFKEAV KNLEWIAGGT WTPSALKFAY N KLIKESRR QKTRVFAVVI TDGRHDPRDD DLNLRALCNH EVTVTAIGIG DMFHEKHESE NL YSIACDK PQQVRNMTLF SDLVAEKFID DMEDVLCPDP QIVCPDLPCQ TELYVAQCTQ RPV DIVFLL DGSERLGEQN FHKVRRFVEE VSRRLTLARK DDDPLNARVA LLQFGGPREQ QVAF PLTSN LTVIQEALAS ARYLNSFSHV GTGIVQAINQ VVQGARAGAR RHAELSFVFL TDGVT GNDS LDEAVHSMRK QNVVPTVVAV GSDVDTDVLS KISLGDPAAV FREKDYDSLA QPGFFD RFI RWIC UniProtKB: Collagen alpha-2(VI) chain |
-Macromolecule #3: Col6a3
Macromolecule | Name: Col6a3 / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Sequence | String: MRKHRHLPLV AILCLFFSGF SFTRGQQQPD VKNGAAADII FLVDSSWSIG KEHFQLVREF LYDVIESLA VGDNDFRFAL VQFNGNPHTE FLFNTYRSKQ EVLSHVSNMS YIGGSNQTGK G LAYVMQNH LTEAAGSRAS DGVPQVIVVL THGHSEDGLA LPSAELKSAD ...String: MRKHRHLPLV AILCLFFSGF SFTRGQQQPD VKNGAAADII FLVDSSWSIG KEHFQLVREF LYDVIESLA VGDNDFRFAL VQFNGNPHTE FLFNTYRSKQ EVLSHVSNMS YIGGSNQTGK G LAYVMQNH LTEAAGSRAS DGVPQVIVVL THGHSEDGLA LPSAELKSAD VNVFAIGVED AD EAALKEI ASEPLNMHVF NLENYTSLHD IVGNLVACVR SSMAPERAGG TEIPKDITAQ DSA DIIFLI DGSNNTGSVN FAVILDFLVN LLERLSIGTQ QIRVGVVQYS DEPRTMFSLN SYST KAQVL DAVKALGFIG GELANVGLAL DFVVENHFTR AGGSRAEEGV PQVLVLISAG PSSDE IRDG VVALKQASVF SFGLGAQAAS KAELQHIATN DNLVFTVPEF RSLGDVQEQL LPYIVG VAQ RHIVLQPPTI VTQVIEVNKR DIVFLVDGSS KLGLTNFNAI RDFIAKVIQR LEIRQDL IQ VAVAQYADTV RPEFYFNTYP SKREVINAVR KMKALDGSAL YTGSALDFVR NNLFTEAA G YRAAEGVPKL LVLVTGGKSL DAVSQPAQEL KRSGILAFAV GNKVADQAEL EEIAFDSSL VFTATEFRPA PLQGVLPGLL GPLRTLTGTT EVRVNKRDII FLLDGSSNVG ETNFPYVRDF VMNLVNSLD VGSDHIRVGL VQFSDTPVTE FSLNTYPTKS ELLAHLRQMQ LQGGSVLNTG A ALSYVHAN HFTEAGGSRI QDHVPQLLLL LTAGQSEDSY LQAANALARA GILTFCVGTS QA DRAELEE IAFNPGLVYL MDDFSSLPAL PQQLIQPLTT YVSGGVEEVP LAQPESKRDI LFL FDGSAN LMGQFTAARD FLYKVIDELD VKPEGTRVAV AQFSDDVKVE SRFDQHQNKP EILN LVKRM KLKTGKALNL GYALDYAQRY IFVKSAGSRI EDGVLQFLVL LVAGKSSDRV DTPAL NLKQ SGVVPFILQA KNADPAELEL IVPSPAFILV AESLPKIGDL QPQIVNLLKS VQNGAP APV SVEKDVVFLI DGSEGVRSGF PLLKEFVQRV VESLDVGPDR VRVAVVQYSD RTRPEFY LN SYMDQQSVVG AIRGLTLLGG PAPNTGAALE FVLRNILVGS AGSRIAEGVP QLLIVLTA D RSGDDVRGPS VVLRRGGAVP IGIGIGNADI TEMQTLSFVP DFAVVIPTFR QLGTIQQVI SERVTQLSRE ELSRLQASVT PLTTPVVSSK RDVVFLIDGS QSAGPEFQYI RTLIERLVDY LDVGFDTTR VAVIQFSDDP RVEFLLNVHS SKDEVQNAVR RLRPKGGRQV NVGGALEYVA R NIFKRPLG SRIEEGVPQF LVLISSGKSD DEVEDSAIEL KQFGVAPLTI ARNVDQEELV KI SLSPEYV FSVNTFRELP SLEQKLLTPL TTLTAGQIQQ LLASTRYPPP AVESDAADIV FLI DSSDGV KPDGIAHIRD FVIRIVRRLN VGPNKVRIGV LQFSNDVFPE FQLKTYKSQA SVLD AIRRL RFKGGSPLNT GKALEFVARN YFVKSAGSRI EDGVPQHLVL FLGGKSQDDI SRYSQ VIKS AGIASLGVGD RNIDRTELQT ITSDPRLVFT VREFRDLPSI EERMVNSFGS SGVTPA PPG VDTPSPSRPE KKKADIVFLL DGSINFRRDS FQEVLRFVSE IVDTVYEGGD SIQVGLV QY NSDPTDEFFL KDFPTKQQII DAINKVVYKG GRHANTKVGL EHLRRNHFVP EAGSRLDQ R VPQIAFVITG GKSVEDAQEA SMALTQRGVK VFAVGVRNID SEEVGKIASN SATAFRVGN VQELSELSEQ VLETLHDAMH ETLCPGVTDV SKACNLDVIL GFDGSGDQNV FVAQKGLEPK VDTILRRIS QMQKISCSGS QLPTVRVSVV ALTPSGPVEA FDFAEYQPEL FEKFQNMRAQ H PYVLTADT LKLYQNKFRQ ASMDNVKVVI HFTDGVDGDL ADLQRASEEL RQEGVRALIL VG LERVANL EQLMQLEFGR GFTYNRPLRL NLLDLDYELA EQLDNIAEKA CCGIPCKCSG QRG DRGPIG SIGPKGIPGE DGYRGYPGDE GGPGERGPPG VNGTQGFQGC PGQRGVKGSR GFPG EKGEL GEIGLDGLDG EDGDKGLPGT SGEKGSPGRR GDKGPKGDKG ERGDVGIRGD PGNSG QDSQ QRGAKGETGD IGPVVQCSPF LPVQSNLPLC GSCGGRGGSP PRSTYVGILL LQGPPG PTG PPGLIGEQGI PGPRVSLAWT LSKSGEPGDP GPKGSIGNRG PRGETGDDGR DGVGSEG RI GKKVFICRGG NPGEPGTDGP PGPKGIRGRR GNSGPPGIAG QKGDPGYPGP SGYKGSRG D SMDQCALVQS IKDKCRPLEC PVFPTELAFA LDTSEGVTQD RFSQMREVVL KILDDLTIA ESNCPRGARV AVVTYNNEVT TEIRFADSKK KSVLLDKIKN LQVSLTSKQQ SLETAMSFVA RNTFKRVRS GFLMRKVAVF FSNKPTRATP QLREAVLKLS DAGITPLFLT SQEDRQLINA L QINNTAVG HALVLPAGGD LTDFLKNVLT CHVCLDICNI DPSCGFGSWR PSFRDRRAAG SD VDIDMAF ILDSSESTTP FQFNEMRKYI EYLVRQLDVS PDPKASQHFA RVAVVQHAPY EAV DNASVP PVKVEFSLTD YGSKEKLLAF LGSRMTQLQG TRALGRAIDY TIENIFESAP NPRD LKIVV LMLTGEVQKQ QLEEAQRAIL QAKCKGYFFV ILGIGRKVNV KELYSSASEP NDVFF KLVD KSTELNEEPL MRFGRLLPSF VSSKDAFYLS PDIRKQCDWF QADQPAKNLV QFGYKQ INV PNNVTSSPTS KLVTTTKPVI TTTKPITVVN LPASKPAATR PVDERPAAGR SVATKMD SA RPVATKTEAT KPAAAAKPAA AKPAPARPPT AARSMATRSE APRPQAVKLA ASRPGAAK P VVKAPREIHV SEVTENSAKL HWERPEPPSP YLYNLTVTSA HDQAVVLKQN LTVTDRVIG GLLPGQTYHV TVTCSLRSQV RAIYQGSFST KKIQPPPPQT ERSASSATIN LVVSADRLAG SKADICKLP KDGGTCREFV LKWYYDSVTE NCARFWYGGC GGNENRFNSQ DECEKVCPPV P IKQPGVIA AMGT UniProtKB: Collagen alpha-3(VI) chain |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 Component:
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Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY ARRAY / Pretreatment - Type: GLOW DISCHARGE | ||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | TFS KRIOS |
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Specialist optics | Energy filter - Slit width: 20 eV |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 29595 / Average exposure time: 2.3 sec. / Average electron dose: 22.165 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.75 µm / Nominal magnification: 105000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |