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Yorodumi- EMDB-26624: Composite cryo-EM density map of the 48-nm repeat of the human re... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-26624 | |||||||||||||||||||||
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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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Function / homology | Function and homology information 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 / regulation of calcineurin-NFAT signaling cascade / sperm axoneme assembly / inner dynein arm assembly / cilium-dependent cell motility / protein polyglutamylation ...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 / regulation of calcineurin-NFAT signaling cascade / sperm axoneme assembly / inner dynein arm assembly / cilium-dependent cell motility / protein polyglutamylation / regulation of microtubule nucleation / positive regulation of feeding behavior / cerebrospinal fluid circulation / sperm principal piece / regulation of cilium beat frequency involved in ciliary motility / cilium movement involved in cell motility / 9+2 motile cilium / regulation of store-operated calcium entry / cilium movement / Transferases; Transferring phosphorus-containing groups / calcium ion sensor activity / acrosomal membrane / axoneme assembly / Post-chaperonin tubulin folding pathway / flagellated sperm motility / cilium organization / axonemal microtubule / left/right axis specification / Carboxyterminal post-translational modifications of tubulin / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Cilium Assembly / gamma-tubulin ring complex / organelle transport along microtubule / glial cell differentiation / forebrain morphogenesis / cytoskeleton-dependent intracellular transport / Sealing of the nuclear envelope (NE) by ESCRT-III / Intraflagellar transport / neuron projection arborization / manchette / positive regulation of cilium assembly / Gap junction assembly / cerebellar cortex morphogenesis / Formation of tubulin folding intermediates by CCT/TriC / dentate gyrus development / COPI-independent Golgi-to-ER retrograde traffic / pyramidal neuron differentiation / natural killer cell mediated cytotoxicity / Prefoldin mediated transfer of substrate to CCT/TriC / UTP biosynthetic process / Kinesins / CTP biosynthetic process / Assembly and cell surface presentation of NMDA receptors / motile cilium / positive regulation of cell motility / determination of left/right symmetry / GTP biosynthetic process / centrosome cycle / intermediate filament / motor behavior / COPI-dependent Golgi-to-ER retrograde traffic / microtubule organizing center / response to L-glutamate / ciliary base / smoothened signaling pathway / intercellular bridge / regulation of synapse organization / beta-tubulin binding / regulation of neuron projection development / AMP binding / regulation of cell division / startle response / spermatid development / Recycling pathway of L1 / locomotory exploration behavior / microtubule polymerization / cerebral cortex cell migration / axoneme / single fertilization / mitotic cytokinesis / alpha-tubulin binding / cilium assembly / sperm flagellum / cellular response to UV-C / RHO GTPases activate IQGAPs / cellular response to unfolded protein / MHC class I protein binding / Hedgehog 'off' state / response to tumor necrosis factor / cytoplasmic microtubule / microtubule-based process / COPI-mediated anterograde transport / Activation of AMPK downstream of NMDARs / response to mechanical stimulus / Mitotic Prometaphase / homeostasis of number of cells within a tissue / EML4 and NUDC in mitotic spindle formation / condensed chromosome / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome Similarity search - Function | |||||||||||||||||||||
Biological species | Homo sapiens (human) / human (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: 2022 Title: 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. | |||||||||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
-Related structure data
Related structure data | 7ungMC 7un1C M: atomic model generated by this map C: citing same article (ref.) |
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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_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 | ||||||||||||||||||||
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
-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 |
-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 % |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / 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 |
Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |