[English] 日本語

- PDB-8i7r: In situ structure of axonemal doublet microtubules in mouse sperm... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 8i7r | ||||||
---|---|---|---|---|---|---|---|
Title | In situ structure of axonemal doublet microtubules in mouse sperm with 48-nm repeat | ||||||
![]() |
| ||||||
![]() | STRUCTURAL PROTEIN / microtubules / axoneme / sperm / filament | ||||||
Function / homology | ![]() male germ-line stem cell population maintenance / left/right pattern formation / epithelial cilium movement involved in determination of left/right asymmetry / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Cilium Assembly / Sealing of the nuclear envelope (NE) by ESCRT-III / 9+0 motile cilium / outer acrosomal membrane / sperm flagellum assembly / regulation of brood size ...male germ-line stem cell population maintenance / left/right pattern formation / epithelial cilium movement involved in determination of left/right asymmetry / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Cilium Assembly / Sealing of the nuclear envelope (NE) by ESCRT-III / 9+0 motile cilium / outer acrosomal membrane / sperm flagellum assembly / regulation of brood size / establishment of left/right asymmetry / axonemal microtubule doublet inner sheath / protein localization to motile cilium / manchette assembly / axonemal B tubule inner sheath / axonemal A tubule inner sheath / Intraflagellar transport / inner dynein arm assembly / regulation of calcineurin-NFAT signaling cascade / Carboxyterminal post-translational modifications of tubulin / sperm axoneme assembly / protein polyglutamylation / positive regulation of feeding behavior / sperm principal piece / COPI-independent Golgi-to-ER retrograde traffic / cerebrospinal fluid circulation / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / microtubule sliding / MAP kinase tyrosine/serine/threonine phosphatase activity / epithelial cilium movement involved in extracellular fluid movement / regulation of store-operated calcium entry / cilium movement involved in cell motility / regulation of cilium beat frequency involved in ciliary motility / COPI-mediated anterograde transport / Aggrephagy / protein localization to organelle / 9+2 motile cilium / Kinesins / Transferases; Transferring phosphorus-containing groups / acrosomal membrane / intraciliary transport / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / PKR-mediated signaling / Resolution of Sister Chromatid Cohesion / cilium movement / The role of GTSE1 in G2/M progression after G2 checkpoint / ciliary transition zone / RHO GTPases activate IQGAPs / axoneme assembly / Recycling pathway of L1 / calcium ion sensor activity / cilium organization / left/right axis specification / axonemal microtubule / COPI-dependent Golgi-to-ER retrograde traffic / RHO GTPases Activate Formins / Separation of Sister Chromatids / gamma-tubulin ring complex / Hedgehog 'off' state / Loss of Nlp from mitotic centrosomes / Recruitment of mitotic centrosome proteins and complexes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / Regulation of PLK1 Activity at G2/M Transition / manchette / flagellated sperm motility / positive regulation of cilium assembly / MHC class II antigen presentation / cell projection organization / protein targeting to mitochondrion / UTP biosynthetic process / CTP biosynthetic process / determination of left/right symmetry / protein targeting to membrane / microtubule organizing center / nucleoside diphosphate kinase activity / extrinsic component of membrane / ciliary base / intermediate filament / GTP biosynthetic process / tubulin complex / positive regulation of cell motility / myosin phosphatase activity / intercellular bridge / protein-serine/threonine phosphatase / cytoplasmic microtubule / receptor clustering / AMP binding / beta-tubulin binding / phosphatase activity / regulation of cell division / axoneme / mitotic cytokinesis / phosphoprotein phosphatase activity / peptidyl-tyrosine dephosphorylation / centriolar satellite / spermatid development Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / subtomogram averaging / cryo EM / Resolution: 6.5 Å | ||||||
![]() | Zhu, Y. / Yin, G.L. / Tai, L.H. / Sun, F. | ||||||
Funding support | ![]()
| ||||||
![]() | ![]() Title: In-cell structural insight into the stability of sperm microtubule doublet. Authors: Linhua Tai / Guoliang Yin / Xiaojun Huang / Fei Sun / Yun Zhu / ![]() Abstract: The propulsion for mammalian sperm swimming is generated by flagella beating. Microtubule doublets (DMTs) along with microtubule inner proteins (MIPs) are essential structural blocks of flagella. ...The propulsion for mammalian sperm swimming is generated by flagella beating. Microtubule doublets (DMTs) along with microtubule inner proteins (MIPs) are essential structural blocks of flagella. However, the intricate molecular architecture of intact sperm DMT remains elusive. Here, by in situ cryo-electron tomography, we solved the in-cell structure of mouse sperm DMT at 4.5-7.5 Å resolutions, and built its model with 36 kinds of MIPs in 48 nm periodicity. We identified multiple copies of Tektin5 that reinforce Tektin bundle, and multiple MIPs with different periodicities that anchor the Tektin bundle to tubulin wall. This architecture contributes to a superior stability of A-tubule than B-tubule of DMT, which was revealed by structural comparison of DMTs from the intact and deformed axonemes. Our work provides an overall molecular picture of intact sperm DMT in 48 nm periodicity that is essential to understand the molecular mechanism of sperm motility as well as the related ciliopathies. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 27.1 MB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 23.2 MB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 22.2 MB | Display | |
Data in XML | ![]() | 3 MB | Display | |
Data in CIF | ![]() | 4.9 MB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 35230MC ![]() 8i7oC C: citing same article ( M: map data used to model this data |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
-
Assembly
Deposited unit | ![]()
|
---|---|
1 |
|
-
Components
+Protein , 24 types, 416 molecules ABA1A2A3A4ABADAFAHAJALBBBDBFBHBJBLCBCDCFCHCJCLDBDDDFDHDJDL...
-EF-hand domain-containing family member ... , 2 types, 5 molecules EFG4G5G6
#9: Protein | Mass: 95891.961 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #14: Protein | Mass: 87758.023 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
---|
-Cilia- and flagella-associated protein ... , 10 types, 27 molecules GHIJKLN1N2N3N4P1P2P3UVWXXAXBXCXDXEXFXGYZa
#12: Protein | Mass: 62036.609 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #16: Protein | | Mass: 26633.035 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #18: Protein | | Mass: 23062.510 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #20: Protein | Mass: 34433.383 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #26: Protein | Mass: 18960.092 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #29: Protein | Mass: 68322.164 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #33: Protein | Mass: 65962.016 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #34: Protein | Mass: 22781.389 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #36: Protein | Mass: 65266.520 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #38: Protein | | Mass: 12278.145 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
---|
-Piercer of microtubule wall ... , 2 types, 2 molecules MN
#23: Protein | Mass: 18862.852 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
---|---|
#25: Protein | Mass: 13728.513 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Non-polymers , 1 types, 279 molecules 
#39: Chemical | ChemComp-GTP / |
---|
-Details
Has ligand of interest | N |
---|
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
---|---|
EM experiment | Aggregation state: CELL / 3D reconstruction method: subtomogram averaging |
-
Sample preparation
Component | Name: mouse sperm / Type: CELL / Entity ID: #1-#38 / Source: NATURAL |
---|---|
Source (natural) | Organism: ![]() ![]() |
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: Titan Krios / Image courtesy: FEI Company |
---|---|
Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
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) |
-
Processing
Software | Name: UCSF ChimeraX / Version: 1.6/v9 / Classification: model building / URL: https://www.rbvi.ucsf.edu/chimerax/ / Os: Windows / Type: package |
---|---|
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
Symmetry | Point symmetry: C1 (asymmetric) |
3D reconstruction | Resolution: 6.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 17450 / Symmetry type: POINT |
EM volume selection | Num. of tomograms: 689 / Num. of volumes extracted: 17450 |