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Yorodumi- EMDB-26624: Composite cryo-EM density map of the 48-nm repeat of the human re... -
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Open data
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Basic information
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| Title | Composite cryo-EM density map of the 48-nm repeat of the human respiratory doublet microtubule | |||||||||||||||||||||
Map data | phenix auto-sharpened map | |||||||||||||||||||||
Sample |
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Keywords | cilia / microtubule / sperm / cell motility / STRUCTURAL PROTEIN | |||||||||||||||||||||
| Function / homology | Function and homology informationaxonemal microtubule doublet inner sheath / outer acrosomal membrane / epithelial cilium movement involved in determination of left/right asymmetry / regulation of brood size / establishment of left/right asymmetry / 9+0 motile cilium / sperm flagellum assembly / manchette assembly / axonemal B tubule inner sheath / axonemal A tubule inner sheath ...axonemal microtubule doublet inner sheath / outer acrosomal membrane / epithelial cilium movement involved in determination of left/right asymmetry / regulation of brood size / establishment of left/right asymmetry / 9+0 motile cilium / sperm flagellum assembly / manchette assembly / axonemal B tubule inner sheath / axonemal A tubule inner sheath / protein polyglutamylation / inner dynein arm assembly / regulation of calcineurin-NFAT signaling cascade / sperm axoneme assembly / regulation of microtubule nucleation / positive regulation of feeding behavior / cilium-dependent cell motility / Transferases; Transferring phosphorus-containing groups / sperm principal piece / regulation of cilium beat frequency involved in ciliary motility / cerebrospinal fluid circulation / epithelial cilium movement involved in extracellular fluid movement / cilium movement involved in cell motility / 9+2 motile cilium / regulation of store-operated calcium entry / intraciliary transport / acrosomal membrane / axoneme assembly / microtubule sliding / cilium movement / ciliary transition zone / left/right axis specification / Post-chaperonin tubulin folding pathway / calcium ion sensor activity / axonemal microtubule / Cilium Assembly / cytoskeleton-dependent intracellular transport / organelle transport along microtubule / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / cilium organization / Carboxyterminal post-translational modifications of tubulin / forebrain morphogenesis / gamma-tubulin ring complex / manchette / Intraflagellar transport / Sealing of the nuclear envelope (NE) by ESCRT-III / cerebellar cortex morphogenesis / glial cell differentiation / dentate gyrus development / positive regulation of cilium assembly / Formation of tubulin folding intermediates by CCT/TriC / neuron projection arborization / flagellated sperm motility / Gap junction assembly / Prefoldin mediated transfer of substrate to CCT/TriC / UTP biosynthetic process / CTP biosynthetic process / Kinesins / COPI-independent Golgi-to-ER retrograde traffic / Assembly and cell surface presentation of NMDA receptors / determination of left/right symmetry / response to L-glutamate / pyramidal neuron differentiation / intermediate filament / centrosome cycle / positive regulation of cell motility / COPI-dependent Golgi-to-ER retrograde traffic / motile cilium / GTP biosynthetic process / smoothened signaling pathway / natural killer cell mediated cytotoxicity / AMP binding / ciliary base / regulation of synapse organization / receptor clustering / regulation of neuron projection development / startle response / motor behavior / cerebral cortex cell migration / response to tumor necrosis factor / Recycling pathway of L1 / locomotory exploration behavior / microtubule polymerization / microtubule organizing center / MHC class I protein binding / regulation of cell division / mitotic cytokinesis / cellular response to UV-C / axoneme / cilium assembly / glial cell projection / spermatid development / cellular response to unfolded protein / sperm flagellum / response to mechanical stimulus / alpha-tubulin binding / single fertilization / RHO GTPases activate IQGAPs / beta-tubulin binding / microtubule-based process Similarity search - Function | |||||||||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||||||||||||||
Authors | Gui M / Croft JT / Zabeo D / Acharya V / Kollman JM / Burgoyne T / Hoog JL / Brown A | |||||||||||||||||||||
| Funding support | United States, Sweden, 6 items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2022Title: SPACA9 is a lumenal protein of human ciliary singlet and doublet microtubules. Authors: Miao Gui / Jacob T Croft / Davide Zabeo / Vajradhar Acharya / Justin M Kollman / Thomas Burgoyne / Johanna L Höög / Alan Brown / ![]() Abstract: The cilium-centrosome complex contains triplet, doublet, and singlet microtubules. The lumenal surfaces of each microtubule within this diverse array are decorated by microtubule inner proteins ...The cilium-centrosome complex contains triplet, doublet, and singlet microtubules. The lumenal surfaces of each microtubule within this diverse array are decorated by microtubule inner proteins (MIPs). Here, we used single-particle cryo-electron microscopy methods to build atomic models of two types of human ciliary microtubule: the doublet microtubules of multiciliated respiratory cells and the distal singlet microtubules of monoflagellated human spermatozoa. We discover that SPACA9 is a polyspecific MIP capable of binding both microtubule types. SPACA9 forms intralumenal striations in the B tubule of respiratory doublet microtubules and noncontinuous spirals in sperm singlet microtubules. By acquiring new and reanalyzing previous cryo-electron tomography data, we show that SPACA9-like intralumenal striations are common features of different microtubule types in animal cilia. Our structures provide detailed references to help rationalize ciliopathy-causing mutations and position cryo-EM as a tool for the analysis of samples obtained directly from ciliopathy patients. | |||||||||||||||||||||
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Structure visualization
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Downloads & links
-EMDB archive
-Validation report
| Summary document | emd_26624_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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| Full document | emd_26624_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | emd_26624_validation.xml.gz | 25.9 KB | Display | |
| Data in CIF | emd_26624_validation.cif.gz | 34.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-26624 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-26624 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7ungMC ![]() 7un1C M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_26624.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | phenix auto-sharpened map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.37 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
+Mask #1
+Additional map: local masked map
+Additional map: stitched unsharpened map
+Additional map: consensus refined map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: deepEMhancer sharpened map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Additional map: local masked map
+Half map: #2
+Half map: #1
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Sample components
+Entire : Doublet microtubule and associated proteins
+Supramolecule #1: Doublet microtubule and associated proteins
+Macromolecule #1: Protein CFAP95
+Macromolecule #2: EF-hand domain-containing family member B
+Macromolecule #3: Cilia- and flagella-associated protein 53
+Macromolecule #4: Nucleoside diphosphate kinase 7
+Macromolecule #5: Protein CFAP107
+Macromolecule #6: Protein CFAP141
+Macromolecule #7: Tektin-1
+Macromolecule #8: Tubulin alpha-1A chain
+Macromolecule #9: Tubulin beta-4B chain
+Macromolecule #10: Meiosis-specific nuclear structural protein 1
+Macromolecule #11: Tektin-2
+Macromolecule #12: Tektin-3
+Macromolecule #13: Sperm-associated antigen 8
+Macromolecule #14: Tektin-4
+Macromolecule #15: Cilia- and flagella-associated protein 161
+Macromolecule #16: Sperm acrosome-associated protein 9
+Macromolecule #17: Uncharacterized protein C15orf65
+Macromolecule #18: Protein FAM166B
+Macromolecule #19: UPF0686 protein C11orf1
+Macromolecule #20: Isoform 2 of Cilia- and flagella-associated protein 77
+Macromolecule #21: Protein FAM183A
+Macromolecule #22: Uncharacterized protein C5orf49
+Macromolecule #23: Protein FAM166C
+Macromolecule #24: RIB43A-like with coiled-coils protein 2
+Macromolecule #25: EF-hand domain-containing protein 1
+Macromolecule #26: EF-hand domain-containing family member C2
+Macromolecule #27: Cilia- and flagella-associated protein 20
+Macromolecule #28: Parkin coregulated gene protein
+Macromolecule #29: Cilia- and flagella-associated protein 45
+Macromolecule #30: Cilia- and flagella-associated protein 52
+Macromolecule #31: Enkurin
+Macromolecule #32: Protein Flattop
+Macromolecule #33: Protein CFAP210
+Macromolecule #34: Protein CFAP276
+Macromolecule #35: UPF0691 protein C9orf116
+Macromolecule #36: GUANOSINE-5'-TRIPHOSPHATE
+Macromolecule #37: MAGNESIUM ION
+Macromolecule #38: GUANOSINE-5'-DIPHOSPHATE
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | filament |
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Sample preparation
| Buffer | pH: 7.3 |
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| Grid | Model: Quantifoil R2/1 / Pretreatment - Type: GLOW DISCHARGE |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 64000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Homo sapiens (human)
Authors
United States,
Sweden, 6 items
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Processing
FIELD EMISSION GUN


