+Open data
-Basic information
Entry | Database: PDB / ID: 7sgs | ||||||||||||||||||||||||
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Title | Cryo-EM structure of full-length MAP7 bound to the microtubule | ||||||||||||||||||||||||
Components |
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Keywords | STRUCTURAL PROTEIN / microtubule / microtubule-associated protein / cytoskeleton | ||||||||||||||||||||||||
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 / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MHC class II antigen presentation / Recruitment of NuMA to mitotic centrosomes / microtubule associated complex / response to osmotic stress / COPI-mediated anterograde transport / establishment or maintenance of cell polarity / protein localization to plasma membrane / structural constituent of cytoskeleton / microtubule cytoskeleton organization / microtubule cytoskeleton / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / mitotic cell cycle / basolateral plasma membrane / microtubule / axon / signaling receptor binding / GTPase activity / GTP binding / perinuclear region of cytoplasm / structural molecule activity / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||||||||||||||||||||
Biological species | Sus scrofa (pig) Homo sapiens (human) | ||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | ||||||||||||||||||||||||
Authors | Ferro, L.S. / Fang, Q. / Eshun-Wilson, L. / Fernandes, J. / Jack, A. / Farrell, D.P. / Golcuk, M. / Huijben, T. / Costa, K. / Gur, M. ...Ferro, L.S. / Fang, Q. / Eshun-Wilson, L. / Fernandes, J. / Jack, A. / Farrell, D.P. / Golcuk, M. / Huijben, T. / Costa, K. / Gur, M. / DiMaio, F. / Nogales, E. / Yildiz, A. | ||||||||||||||||||||||||
Funding support | United States, 7items
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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
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7sgs.cif.gz | 259 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7sgs.ent.gz | 191.5 KB | Display | PDB format |
PDBx/mmJSON format | 7sgs.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7sgs_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 7sgs_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 7sgs_validation.xml.gz | 38.5 KB | Display | |
Data in CIF | 7sgs_validation.cif.gz | 59.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sg/7sgs ftp://data.pdbj.org/pub/pdb/validation_reports/sg/7sgs | HTTPS FTP |
-Related structure data
Related structure data | 25120MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-Protein , 3 types, 4 molecules BDCA
#1: Protein | Mass: 50204.445 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sus scrofa (pig) / Gene: TUBA1B / Production host: Escherichia coli (E. coli) / References: UniProt: Q2XVP4 #2: Protein | | Mass: 49907.770 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sus scrofa (pig) / Production host: Escherichia coli (E. coli) / References: UniProt: P02554 #3: Protein | | Mass: 84207.195 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MAP7 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q14244 |
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-Non-polymers , 3 types, 5 molecules
#4: Chemical | #5: Chemical | #6: Chemical | ChemComp-GDP / | |
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-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Ternary complex of alpha-beta tubulin with microtubule-assosiated protein 7 Type: COMPLEX / Entity ID: #1-#3 / Source: MULTIPLE SOURCES |
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Source (natural) | Organism: Sus scrofa (pig) |
Source (recombinant) | Organism: Escherichia coli (E. coli) |
Buffer solution | pH: 7 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Talos Arctica / Image courtesy: FEI Company |
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Microscopy | Model: FEI TALOS ARCTICA |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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Symmetry | Point symmetry: C1 (asymmetric) |
3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 99219 / Symmetry type: POINT |