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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Bovine Flagellar TRiC | |||||||||
Map data | Bovine-Flagellar-TRiC-composite-map | |||||||||
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Keywords | TRiC / sperm / flagella / motile cilia / CHAPERONE | |||||||||
| Function / homology | Function and homology informationAssociation of TriC/CCT with target proteins during biosynthesis / RHOBTB2 GTPase cycle / RHOBTB1 GTPase cycle / zona pellucida receptor complex / positive regulation of establishment of protein localization to telomere / scaRNA localization to Cajal body / positive regulation of telomerase RNA localization to Cajal body / chaperonin-containing T-complex / binding of sperm to zona pellucida / Neutrophil degranulation ...Association of TriC/CCT with target proteins during biosynthesis / RHOBTB2 GTPase cycle / RHOBTB1 GTPase cycle / zona pellucida receptor complex / positive regulation of establishment of protein localization to telomere / scaRNA localization to Cajal body / positive regulation of telomerase RNA localization to Cajal body / chaperonin-containing T-complex / binding of sperm to zona pellucida / Neutrophil degranulation / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / WD40-repeat domain binding / chaperone-mediated protein complex assembly / Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides / beta-tubulin binding / positive regulation of telomere maintenance via telomerase / mRNA 3'-UTR binding / ATP-dependent protein folding chaperone / mRNA 5'-UTR binding / response to virus / : / melanosome / G-protein beta-subunit binding / protein folding / cell body / microtubule / protein stabilization / ubiquitin protein ligase binding / centrosome / ATP hydrolysis activity / ATP binding / metal ion binding / identical protein binding Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
Authors | Cong Y / Meng X | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Mol Cell / Year: 2026Title: Chaperonin TRiC bridges radial spokes for folding locally translated proteins to sustain mammalian sperm flagellar motility. Authors: Xueming Meng / Luan Li / Cheng Lin / Yun Zhu / Yanyan Feng / Qun Zhao / Nan Zhao / Xuehai Zhou / Yujie Tong / Shanshan Wang / Guoliang Yin / Ruimin Liu / Lihua Zhang / Fei Sun / Xiumin Yan / ...Authors: Xueming Meng / Luan Li / Cheng Lin / Yun Zhu / Yanyan Feng / Qun Zhao / Nan Zhao / Xuehai Zhou / Yujie Tong / Shanshan Wang / Guoliang Yin / Ruimin Liu / Lihua Zhang / Fei Sun / Xiumin Yan / Xueliang Zhu / Yao Cong / ![]() Abstract: As animals evolved from external to internal fertilization, sperm flagella, once transiently propelling sperm in water to reach nearby eggs, developed to beat for days in the viscous female ...As animals evolved from external to internal fertilization, sperm flagella, once transiently propelling sperm in water to reach nearby eggs, developed to beat for days in the viscous female reproductive tract. How flagella are remodeled accordingly remains unclear. Unlike externally fertilizing zebrafish and sea urchins, mammalian flagella feature a barrel between radial spokes (RSs) RS1 and RS2. Here, we show that this RS1-RS2 barrel (RRB) is a unique T-complex protein-1 ring complex (TRiC) that folds locally translated polypeptides to sustain flagellar motility. Cryo-electron microscopy (cryo-EM) reveals a flagellum-specific TRiC structure. An in situ cryo-electron tomography (cryo-ET) map of flagellar axonemes captures the RRB TRiC in an active, substrate-receptive state, with additional densities suggestive of folding substrates and cofactors. Mammalian flagella contain components of translation machineries and locally synthesize proteins. Cross-linking mass spectrometry identifies candidate locally translated axonemal proteins and folding substrates. Furthermore, a TRiC ATPase inhibitor markedly represses mouse sperm motility. Our findings provide insights into flagellar remodeling in internally fertilizing species. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_62249.map.gz | 12.8 MB | EMDB map data format | |
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| Header (meta data) | emd-62249-v30.xml emd-62249.xml | 26.1 KB 26.1 KB | Display Display | EMDB header |
| Images | emd_62249.png | 182.4 KB | ||
| Filedesc metadata | emd-62249.cif.gz | 8.9 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-62249 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-62249 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9kcfMC C: citing same article ( M: atomic model generated by this map |
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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_62249.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Bovine-Flagellar-TRiC-composite-map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.8657 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
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Sample components
+Entire : TRiC purified from bovine sperm flagella
+Supramolecule #1: TRiC purified from bovine sperm flagella
+Macromolecule #1: Probable T-complex protein 1 subunit zeta-2
+Macromolecule #2: T-complex protein 1 subunit eta
+Macromolecule #3: T-complex protein 1 subunit alpha
+Macromolecule #4: T-complex protein 1 subunit beta
+Macromolecule #5: T-complex protein 1 subunit gamma
+Macromolecule #6: T-complex protein 1 subunit delta
+Macromolecule #7: T-complex protein 1 subunit epsilon
+Macromolecule #8: T-complex protein 1 subunit theta
+Macromolecule #9: T-complex protein 1 subunit zeta
+Macromolecule #10: MAGNESIUM ION
+Macromolecule #11: ADENOSINE-5'-DIPHOSPHATE
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.4 |
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| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 54.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 0.01 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Keywords
Authors
China, 1 items
Citation






Z (Sec.)
Y (Row.)
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Processing
FIELD EMISSION GUN


