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Open data
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Basic information
| Entry | Database: PDB / ID: 7ung | |||||||||||||||||||||
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| Title | 48-nm repeat of the human respiratory doublet microtubule | |||||||||||||||||||||
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Keywords | STRUCTURAL PROTEIN / cilia / microtubule / sperm / cell motility | |||||||||||||||||||||
| 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 / positive regulation of cilium assembly / Formation of tubulin folding intermediates by CCT/TriC / glial cell differentiation / dentate gyrus development / 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 / determination of left/right symmetry / Assembly and cell surface presentation of NMDA receptors / response to L-glutamate / intermediate filament / pyramidal neuron differentiation / 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 / MHC class I protein binding / regulation of cell division / microtubule organizing center / mitotic cytokinesis / cellular response to UV-C / axoneme / cilium assembly / glial cell projection / spermatid development / cellular response to unfolded protein / response to mechanical stimulus / single fertilization / sperm flagellum / alpha-tubulin binding / RHO GTPases activate IQGAPs / beta-tubulin binding / microtubule-based process Similarity search - Function | |||||||||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||||||||||||||
Authors | Gui, M. / Croft, J.T. / Zabeo, D. / Acharya, V. / Kollman, J.M. / Burgoyne, T. / Hoog, J.L. / Brown, A. | |||||||||||||||||||||
| Funding support | United States, Sweden, 6items
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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
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7ung.cif.gz | 26.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7ung.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 7ung.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7ung_validation.pdf.gz | 19.3 MB | Display | wwPDB validaton report |
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| Full document | 7ung_full_validation.pdf.gz | 19.8 MB | Display | |
| Data in XML | 7ung_validation.xml.gz | 3.3 MB | Display | |
| Data in CIF | 7ung_validation.cif.gz | 5.3 MB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/un/7ung ftp://data.pdbj.org/pub/pdb/validation_reports/un/7ung | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 26624MC ![]() 7un1C M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
+Protein , 26 types, 408 molecules 075689AA0A1A2A3A4AAACAEAGAIAKAMBABCBEBGBIBKBMCACCCECG...
-EF-hand domain-containing family member ... , 2 types, 6 molecules 12WXYZ
| #2: Protein | Mass: 93940.008 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q8N7U6#26: Protein | Mass: 87516.828 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q5JST6 |
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-Cilia- and flagella-associated protein ... , 5 types, 18 molecules 34EFXAXBXCXDXEXFXGabcdefg
| #3: Protein | Mass: 61960.844 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96M91#15: Protein | Mass: 34339.973 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q6P656#27: Protein | Mass: 22807.469 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y6A4#29: Protein | Mass: 65858.109 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9UL16#30: Protein | Mass: 68379.062 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q8N1V2 |
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-Uncharacterized protein ... , 2 types, 3 molecules GL1L2
| #17: Protein | Mass: 13778.468 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: H3BRN8 |
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| #22: Protein | Mass: 17019.980 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: A4QMS7 |
-Non-polymers , 3 types, 451 molecules 




| #36: Chemical | ChemComp-GTP / #37: Chemical | ChemComp-MG / #38: 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 |
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Sample preparation
| Component | Name: Doublet microtubule and associated proteins / Type: COMPLEX / Entity ID: #1-#35 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.3 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid type: Quantifoil R2/1 |
| Vitrification | Cryogen name: ETHANE / Humidity: 100 % |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 64000 X / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm / Alignment procedure: COMA FREE |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||
| 3D reconstruction | Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 208558 / Symmetry type: POINT |
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About Yorodumi




Homo sapiens (human)
United States,
Sweden, 6items
Citation







PDBj



























FIELD EMISSION GUN