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- EMDB-62230: TRiC purified from bovine sperm flagella, concensus map -

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Basic information

Entry
Database: EMDB / ID: EMD-62230
TitleTRiC purified from bovine sperm flagella, concensus map
Map dataBovine-flagellar-TRiC_Consensus_map
Sample
  • Complex: TRiC purified from bovine sperm flagella
KeywordsTRiC / sperm / flagella / motile cilia / CHAPERONE
Biological speciesBos taurus (domestic cattle)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.59 Å
AuthorsMeng X / Cong Y
Funding support China, 1 items
OrganizationGrant numberCountry
Chinese Academy of Sciences China
CitationJournal: Mol Cell / Year: 2026
Title: 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.
History
DepositionNov 1, 2024-
Header (metadata) releaseApr 29, 2026-
Map releaseApr 29, 2026-
UpdateApr 29, 2026-
Current statusApr 29, 2026Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_62230.png

Downloads & links

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Map

FileDownload / File: emd_62230.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationBovine-flagellar-TRiC_Consensus_map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.87 Å/pix.
x 400 pix.
= 346.28 Å		0.87 Å/pix.
x 400 pix.
= 346.28 Å		0.87 Å/pix.
x 400 pix.
= 346.28 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.8657 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.06
Minimum - Maximum-0.1642579 - 0.4850458
Average (Standard dev.)0.0008067769 (±0.016582873)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 346.28 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_62230_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Bovine-flagellar-TRiC Consensus map J591 map half A

Fileemd_62230_half_map_1.map
AnnotationBovine-flagellar-TRiC_Consensus_map_J591_map_half_A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Bovine-flagellar-TRiC Consensus map J591 map half B

Fileemd_62230_half_map_2.map
AnnotationBovine-flagellar-TRiC_Consensus_map_J591_map_half_B
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : TRiC purified from bovine sperm flagella

EntireName: TRiC purified from bovine sperm flagella
Components
  • Complex: TRiC purified from bovine sperm flagella

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Supramolecule #1: TRiC purified from bovine sperm flagella

SupramoleculeName: TRiC purified from bovine sperm flagella / type: complex / ID: 1 / Parent: 0
Source (natural)Organism: Bos taurus (domestic cattle)

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 54.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 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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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.59 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 130150
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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