+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-25120 | ||||||||||||||||||||||||
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Title | Cryo-EM structure of full-length MAP7 bound to the microtubule | ||||||||||||||||||||||||
Map data | |||||||||||||||||||||||||
Sample |
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Keywords | microtubule / microtubule-associated protein / cytoskeleton / STRUCTURAL PROTEIN | ||||||||||||||||||||||||
Function / homology | Function and homology information Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Hedgehog 'off' state / Cilium Assembly / Intraflagellar transport / COPI-dependent Golgi-to-ER retrograde traffic / Carboxyterminal post-translational modifications of tubulin / RHOH GTPase cycle / Sealing of the nuclear envelope (NE) by ESCRT-III / Kinesins / PKR-mediated signaling ...Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Hedgehog 'off' state / Cilium Assembly / Intraflagellar transport / COPI-dependent Golgi-to-ER retrograde traffic / Carboxyterminal post-translational modifications of tubulin / RHOH GTPase cycle / Sealing of the nuclear envelope (NE) by ESCRT-III / Kinesins / PKR-mediated signaling / The role of GTSE1 in G2/M progression after G2 checkpoint / Aggrephagy / Resolution of Sister Chromatid Cohesion / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Separation of Sister Chromatids / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / Recruitment of NuMA to mitotic centrosomes / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MHC class II antigen presentation / microtubule associated complex / response to osmotic stress / COPI-mediated anterograde transport / establishment or maintenance of cell polarity / protein localization to plasma membrane / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / structural constituent of cytoskeleton / microtubule cytoskeleton organization / microtubule cytoskeleton / mitotic cell cycle / basolateral plasma membrane / microtubule / axon / signaling receptor binding / GTPase activity / GTP binding / structural molecule activity / perinuclear region of cytoplasm / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||||||||
Biological species | Sus scrofa (pig) / Homo sapiens (human) | ||||||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | ||||||||||||||||||||||||
Authors | Ferro LS / Fang Q | ||||||||||||||||||||||||
Funding support | United States, 7 items
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Citation | Journal: Science / Year: 2022 Title: Structural and functional insight into regulation of kinesin-1 by microtubule-associated protein MAP7. Authors: Luke S Ferro / Qianglin Fang / Lisa Eshun-Wilson / Jonathan Fernandes / Amanda Jack / Daniel P Farrell / Mert Golcuk / Teun Huijben / Katelyn Costa / Mert Gur / Frank DiMaio / Eva Nogales / Ahmet Yildiz / Abstract: Microtubule (MT)-associated protein 7 (MAP7) is a required cofactor for kinesin-1-driven transport of intracellular cargoes. Using cryo-electron microscopy and single-molecule imaging, we ...Microtubule (MT)-associated protein 7 (MAP7) is a required cofactor for kinesin-1-driven transport of intracellular cargoes. Using cryo-electron microscopy and single-molecule imaging, we investigated how MAP7 binds MTs and facilitates kinesin-1 motility. The MT-binding domain (MTBD) of MAP7 bound MTs as an extended α helix between the protofilament ridge and the site of lateral contact. Unexpectedly, the MTBD partially overlapped with the binding site of kinesin-1 and inhibited its motility. However, by tethering kinesin-1 to the MT, the projection domain of MAP7 prevented dissociation of the motor and facilitated its binding to available neighboring sites. The inhibitory effect of the MTBD dominated as MTs became saturated with MAP7. Our results reveal biphasic regulation of kinesin-1 by MAP7 in the context of their competitive binding to MTs. | ||||||||||||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_25120.map.gz | 10.6 MB | EMDB map data format | |
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Header (meta data) | emd-25120-v30.xml emd-25120.xml | 18.7 KB 18.7 KB | Display Display | EMDB header |
Images | emd_25120.png | 93.1 KB | ||
Filedesc metadata | emd-25120.cif.gz | 6.7 KB | ||
Others | emd_25120_additional_1.map.gz | 130.2 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-25120 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-25120 | HTTPS FTP |
-Validation report
Summary document | emd_25120_validation.pdf.gz | 525.5 KB | Display | EMDB validaton report |
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Full document | emd_25120_full_validation.pdf.gz | 525.1 KB | Display | |
Data in XML | emd_25120_validation.xml.gz | 5.7 KB | Display | |
Data in CIF | emd_25120_validation.cif.gz | 6.4 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-25120 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-25120 | HTTPS FTP |
-Related structure data
Related structure data | 7sgsMC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_25120.map.gz / Format: CCP4 / Size: 11.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Voxel size | X=Y=Z: 1.14 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: Cryo-EM map of FL-MAP7 before symmetry expansion
File | emd_25120_additional_1.map | ||||||||||||
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Annotation | Cryo-EM map of FL-MAP7 before symmetry expansion | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Ternary complex of alpha-beta tubulin with microtubule-assosiated...
Entire | Name: Ternary complex of alpha-beta tubulin with microtubule-assosiated protein 7 |
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Components |
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-Supramolecule #1: Ternary complex of alpha-beta tubulin with microtubule-assosiated...
Supramolecule | Name: Ternary complex of alpha-beta tubulin with microtubule-assosiated protein 7 type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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Source (natural) | Organism: Sus scrofa (pig) |
-Macromolecule #1: Tubulin alpha-1B chain
Macromolecule | Name: Tubulin alpha-1B chain / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Sus scrofa (pig) |
Molecular weight | Theoretical: 50.204445 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHP EQLITGKEDA ANNYARGHYT IGKEIIDLVL DRIRKLADQC TGLQGFLVFH SFGGGTGSGF TSLLMERLSV D YGKKSKLE ...String: MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHP EQLITGKEDA ANNYARGHYT IGKEIIDLVL DRIRKLADQC TGLQGFLVFH SFGGGTGSGF TSLLMERLSV D YGKKSKLE FSIYPAPQVS TAVVEPYNSI LTTHTTLEHS DCAFMVDNEA IYDICRRNLD IERPTYTNLN RLISQIVSSI TA SLRFDGA LNVDLTEFQT NLVPYPRIHF PLATYAPVIS AEKAYHEQLS VAEITNACFE PANQMVKCDP RHGKYMACCL LYR GDVVPK DVNAAIATIK TKRSIQFVDW CPTGFKVGIN YQPPTVVPGG DLAKVQRAVC MLSNTTAIAE AWARLDHKFD LMYA KRAFV HWYVGEGMEE GEFSEAREDM AALEKDYEEV GVDSVEGEGE EEGEEY UniProtKB: Tubulin alpha-1B chain |
-Macromolecule #2: Tubulin beta chain
Macromolecule | Name: Tubulin beta chain / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Sus scrofa (pig) |
Molecular weight | Theoretical: 49.90777 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEAAGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDN FVFGQSGAGN NWAKGHYTEG AELVDSVLDV VRKESESCDC LQGFQLTHSL GGGTGSGMGT LLISKIREEY P DRIMNTFS ...String: MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEAAGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDN FVFGQSGAGN NWAKGHYTEG AELVDSVLDV VRKESESCDC LQGFQLTHSL GGGTGSGMGT LLISKIREEY P DRIMNTFS VVPSPKVSDT VVEPYNATLS VHQLVENTDE TYCIDNEALY DICFRTLKLT TPTYGDLNHL VSATMSGVTT CL RFPGQLN ADLRKLAVNM VPFPRLHFFM PGFAPLTSRG SQQYRALTVP ELTQQMFDAK NMMAACDPRH GRYLTVAAVF RGR MSMKEV DEQMLNVQNK NSSYFVEWIP NNVKTAVCDI PPRGLKMSAT FIGNSTAIQE LFKRISEQFT AMFRRKAFLH WYTG EGMDE MEFTEAESNM NDLVSEYQQY QDATADEQGE FEEEGEEDEA UniProtKB: Tubulin beta chain |
-Macromolecule #3: Ensconsin
Macromolecule | Name: Ensconsin / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 84.207195 KDa |
Recombinant expression | Organism: Spodoptera frugiperda (fall armyworm) |
Sequence | String: MAELGAGGDG HRGGDGAVRS ETAPDSYKVQ DKKNASSRPA SAISGQNNNH SGNKPDPPPV LRVDDRQRLA RERREEREKQ LAAREIVWL EREERARQHY EKHLEERKKR LEEQRQKEER RRAAVEEKRR QRLEEDKERH EAVVRRTMER SQKPKQKHNR W SWGGSLHG ...String: MAELGAGGDG HRGGDGAVRS ETAPDSYKVQ DKKNASSRPA SAISGQNNNH SGNKPDPPPV LRVDDRQRLA RERREEREKQ LAAREIVWL EREERARQHY EKHLEERKKR LEEQRQKEER RRAAVEEKRR QRLEEDKERH EAVVRRTMER SQKPKQKHNR W SWGGSLHG SPSIHSADPD RRSVSTMNLS KYVDPVISKR LSSSSATLLN SPDRARRLQL SPWESSVVNR LLTPTHSFLA RS KSTAALS GEAASCSPII MPYKAAHSRN SMDRPKLFVT PPEGSSRRRI IHGTASYKKE RERENVLFLT SGTRRAVSPS NPK ARQPAR SRLWLPSKSL PHLPGTPRPT SSLPPGSVKA APAQVRPPSP GNIRPVKREV KVEPEKKDPE KEPQKVANEP SLKG RAPLV KVEEATVEER TPAEPEVGPA APAMAPAPAS APAPASAPAP APVPTPAMVS APSSTVNASA SVKTSAGTTD PEEAT RLLA EKRRLAREQR EKEERERREQ EELERQKREE LAQRVAEERT TRREEESRRL EAEQAREKEE QLQRQAEERA LREREE AER AQRQKEEEAR VREEAERVRQ EREKHFQREE QERLERKKRL EEIMKRTRRT EATDKKTSDQ RNGDIAKGAL TGGTEVS AL PCTTNAPGNG KPVGSPHVVT SHQSKVTVES TPDLEKQPNE NGVSVQNENF EEIINLPIGS KPSRLDVTNS ESPEIPLN P ILAFDDEGTL GPLPQVDGVQ TQQTAEVI UniProtKB: Ensconsin |
-Macromolecule #4: GUANOSINE-5'-TRIPHOSPHATE
Macromolecule | Name: GUANOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 4 / Number of copies: 2 / Formula: GTP |
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Molecular weight | Theoretical: 523.18 Da |
Chemical component information | ChemComp-GTP: |
-Macromolecule #5: MAGNESIUM ION
Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 5 / Number of copies: 2 / Formula: MG |
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Molecular weight | Theoretical: 24.305 Da |
-Macromolecule #6: GUANOSINE-5'-DIPHOSPHATE
Macromolecule | Name: GUANOSINE-5'-DIPHOSPHATE / type: ligand / ID: 6 / Number of copies: 1 / Formula: GDP |
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Molecular weight | Theoretical: 443.201 Da |
Chemical component information | ChemComp-GDP: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | filament |
-Sample preparation
Buffer | pH: 7 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Talos Arctica / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: EMDB MAP |
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Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 99219 |
Initial angle assignment | Type: PROJECTION MATCHING |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |