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Yorodumi- PDB-9ijj: In situ structure of the central apparatus in mouse sperm axoneme. -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9ijj | |||||||||||||||
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| Title | In situ structure of the central apparatus in mouse sperm axoneme. | |||||||||||||||
Components |
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Keywords | PROTEIN TRANSPORT / microtubules / axoneme / sperm / filament | |||||||||||||||
| Function / homology | Function and homology informationcell motility in response to calcium ion / intramanchette transport / maintenance of cell number / substrate-dependent cell migration, cell attachment to substrate / axonemal central pair projection / male germ-line stem cell population maintenance / respiratory system development / organelle disassembly / regulation of cilium beat frequency / axonemal central apparatus ...cell motility in response to calcium ion / intramanchette transport / maintenance of cell number / substrate-dependent cell migration, cell attachment to substrate / axonemal central pair projection / male germ-line stem cell population maintenance / respiratory system development / organelle disassembly / regulation of cilium beat frequency / axonemal central apparatus / regulation of establishment of planar polarity / lateral wall of outer hair cell / axonemal microtubule doublet inner sheath / mucociliary clearance / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Cilium Assembly / Sealing of the nuclear envelope (NE) by ESCRT-III / sperm flagellum assembly / axonemal central apparatus assembly / manchette assembly / positive regulation of fertilization / radial spoke / axonemal B tubule inner sheath / CaMK IV-mediated phosphorylation of CREB / Cam-PDE 1 activation / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Glycogen breakdown (glycogenolysis) / Activation of RAC1 downstream of NMDARs / Sodium/Calcium exchangers / Activation of Ca-permeable Kainate Receptor / positive regulation of flagellated sperm motility / regulation of flagellated sperm motility / Synthesis of IP3 and IP4 in the cytosol / CLEC7A (Dectin-1) induces NFAT activation / RHO GTPases activate PAKs / Carboxyterminal post-translational modifications of tubulin / Calmodulin induced events / Inactivation, recovery and regulation of the phototransduction cascade / Intraflagellar transport / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / eNOS activation / protein polyglutamylation / trachea development / outer dynein arm / beta-adrenergic-receptor kinase / sperm axoneme assembly / positive regulation of feeding behavior / Reduction of cytosolic Ca++ levels / Unblocking of NMDA receptors, glutamate binding and activation / COPI-independent Golgi-to-ER retrograde traffic / Calcineurin activates NFAT / Ion transport by P-type ATPases / Protein methylation / sperm principal piece / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / olfactory behavior / regulation of cilium beat frequency involved in ciliary motility / cerebrospinal fluid circulation / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / RAF activation / epithelial cilium movement involved in extracellular fluid movement / beta-adrenergic receptor kinase activity / G protein-coupled receptor kinase activity / cilium movement involved in cell motility / VEGFR2 mediated vascular permeability / response to odorant / COPI-mediated anterograde transport / sperm head-tail coupling apparatus / Aggrephagy / RAS processing / 9+2 motile cilium / G alpha (s) signalling events / microtubule anchoring at centrosome / Kinesins / PTW/PP1 phosphatase complex / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / metaphase chromosome alignment / Resolution of Sister Chromatid Cohesion / PKR-mediated signaling / acrosomal membrane / Ca2+ pathway / The role of GTSE1 in G2/M progression after G2 checkpoint / axoneme assembly / RHO GTPases activate IQGAPs / microtubule sliding / Recycling pathway of L1 / Extra-nuclear estrogen signaling / FCERI mediated Ca+2 mobilization / cilium movement / RAF/MAP kinase cascade / regulation of nucleocytoplasmic transport / axonemal microtubule / COPI-dependent Golgi-to-ER retrograde traffic / motile cilium assembly / PKA activation / RHO GTPases Activate Formins / regulation of podosome assembly / Separation of Sister Chromatids / cilium organization Similarity search - Function | |||||||||||||||
| Biological species | ![]() | |||||||||||||||
| Method | ELECTRON MICROSCOPY / subtomogram averaging / cryo EM / Resolution: 7.7 Å | |||||||||||||||
Authors | Zhu, Y. / Yin, G. / Sun, F. | |||||||||||||||
| Funding support | China, 1items
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Citation | Journal: Cell Res / Year: 2025Title: In situ structure of the mouse sperm central apparatus reveals mechanistic insights into asthenozoospermia. Authors: Yun Zhu / Tingting Lin / Guoliang Yin / Linhua Tai / Lianwan Chen / Jing Ma / Guoning Huang / Yi Lu / Zhiyong Zhang / Binbin Wang / Suren Chen / Fei Sun / ![]() Abstract: The central apparatus (CA) within the sperm axoneme is vital for sperm motility, yet its molecular architecture and functional mechanisms remain incompletely understood. Combining cryo-electron ...The central apparatus (CA) within the sperm axoneme is vital for sperm motility, yet its molecular architecture and functional mechanisms remain incompletely understood. Combining cryo-electron tomography and AlphaFold2, we resolved the in-cell structure of mouse sperm CA at a subnanometer resolution and built a near-complete atomic model. Our analysis identified 39 CA-associated proteins, including eight previously unreported components. By presenting the full-length structures of CFAP47 and HYDIN, we elucidate their molecular roles in tethering the C1 and C2 microtubules within the CA. Specifically, HYDIN forms a semicircular chain that encircles C1 and C2, with its N-terminal half driving the C1-C2 connection and its C-terminal half providing axial support in C2. CFAP47, the core structural component of the bridge, binds C1 through its N-terminal domains, interacts with HYDIN via its central CFAP47-ring, and anchors to C2 through its C-terminal region. The significantly reduced sperm motility and impaired CA structure observed in Cfap47-knockout mice confirmed the important role of CFAP47. Furthermore, genetic analysis of infertile Chinese men with asthenozoospermia identified previously unreported mutations in the CFAP47. The CA structural model elucidates the pathogenic mechanisms of these mutations, establishing a direct link between CFAP47 dysfunction and impaired sperm motility. Therefore, our study provides mechanistic insights into CA-related fertility disorders. | |||||||||||||||
| History |
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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 | 9ijj.cif.gz | 34.7 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9ijj.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9ijj.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9ijj_validation.pdf.gz | 5.7 MB | Display | wwPDB validaton report |
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| Full document | 9ijj_full_validation.pdf.gz | 9.8 MB | Display | |
| Data in XML | 9ijj_validation.xml.gz | 3.1 MB | Display | |
| Data in CIF | 9ijj_validation.cif.gz | 6.1 MB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ij/9ijj ftp://data.pdbj.org/pub/pdb/validation_reports/ij/9ijj | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 60633MC C: citing same article ( M: map data used to model this data |
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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
-Spermatogenesis-associated protein ... , 2 types, 8 molecules baWXYZ3B3C
| #1: Protein | Mass: 33629.938 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #25: Protein | Mass: 45579.160 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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+Protein , 26 types, 382 molecules cdefgqrsvwFGMOPAbAdAfAhAjBbBdBfBhBjCbCdCfChCj...
-Cilia- and flagella-associated protein ... , 8 types, 26 molecules hijknopmltuCDEHILA2A3A43K3L3M3N3O3P
| #3: Protein | Mass: 209372.391 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 128422.953 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 22781.389 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | Mass: 179171.109 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | Mass: 354209.125 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | | Mass: 97096.742 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #21: Protein | Mass: 106368.562 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #26: Protein | Mass: 37912.082 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Cilia and flagella associated protein ... , 2 types, 5 molecules ABJK5A
| #8: Protein | Mass: 302995.875 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #43: Protein | Mass: 76053.766 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Sperm-associated antigen ... , 3 types, 36 molecules QRSTUVxyzAAABACADAEAFAGAHAIAJAKALAMANAOAPAQARASATAU...
| #15: Protein | Mass: 71570.812 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #16: Protein | Mass: 263465.531 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #19: Protein | Mass: 55329.016 Da / Num. of mol.: 27 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Protein/peptide , 2 types, 2 molecules 3f3g
| #31: Protein/peptide | Mass: 1549.902 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #32: Protein/peptide | Mass: 4017.944 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Leucine-rich repeat and ... , 2 types, 5 molecules 4P4Q4O4X4Y
| #37: Protein | Mass: 93304.680 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #39: Protein | Mass: 97243.797 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Details
| Has protein modification | Y |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: CELL / 3D reconstruction method: subtomogram averaging |
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Sample preparation
| Component | Name: mouse sperm / Type: CELL / Entity ID: all / Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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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: SPOT SCAN |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 5000 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm |
| Image recording | Electron dose: 3 e/Å2 / Avg electron dose per subtomogram: 117 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 QUANTUM (4k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 7.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 19000 / Symmetry type: POINT |
| EM volume selection | Num. of tomograms: 1889 / Num. of volumes extracted: 105000 |
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FIELD EMISSION GUN