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- PDB-9lwo: Cryo-EM structure of the cytosolic ARMH2-EFCAB9-CATSPERz subcompl... -

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Basic information

Entry
Database: PDB / ID: 9lwo
TitleCryo-EM structure of the cytosolic ARMH2-EFCAB9-CATSPERz subcomplex of the mouse CatSpermasome
Components
  • Armadillo-like helical domain containing 2
  • Cation channel sperm-associated auxiliary subunit zeta
  • EF-hand calcium-binding domain-containing protein 9
KeywordsCYTOSOLIC PROTEIN / CatSper / sperm motility / male fertility / channel / ARMH2
Function / homology
Function and homology information


CatSper complex / sperm principal piece / calcium ion sensor activity / male meiotic nuclear division / flagellated sperm motility / sperm capacitation / spermatogenesis / calmodulin binding / calcium ion binding / cytoplasm
Similarity search - Function
Armadillo-like helical domain-containing protein 2 / Armadillo-like helical domain-containing protein 2 / Cation channel sperm-associated auxiliary subunit zeta / EF-hand calcium-binding domain-containing protein 9 / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair
Similarity search - Domain/homology
Armadillo-like helical domain containing 2 / Cation channel sperm-associated auxiliary subunit zeta / EF-hand calcium-binding domain-containing protein 9
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.77 Å
AuthorsZhao, Q. / Lin, S. / Xu, Q. / Wu, J.
Funding support China, 1items
OrganizationGrant numberCountry
National Science Foundation (NSF, China)32271261 China
CitationJournal: Nat Commun / Year: 2025
Title: ARMH2 is a cytosolic component of CatSper crucial for sperm function.
Authors: Qingqing Zhao / Shiyi Lin / Hang Kang / Yanfei Ru / Qikui Xu / Zijing Yu / Xiaofang Huang / Carlo De Rito / Giulia Sassi / Shaojie Wang / Shuya Sun / Rui Sun / Honghan Cheng / Yi Zhu / ...Authors: Qingqing Zhao / Shiyi Lin / Hang Kang / Yanfei Ru / Qikui Xu / Zijing Yu / Xiaofang Huang / Carlo De Rito / Giulia Sassi / Shaojie Wang / Shuya Sun / Rui Sun / Honghan Cheng / Yi Zhu / Mingxi Liu / Yongdeng Zhang / Min Jiang / Riccardo Percudani / Jean-Ju Chung / Xuhui Zeng / Zhen Yan / Jianping Wu /
Abstract: Sperm capacitation and fertilization are highly regulated by Ca signaling. CatSper, a sperm-specific calcium channel, plays a crucial role in sperm hyperactivated motility and fertility by mediating ...Sperm capacitation and fertilization are highly regulated by Ca signaling. CatSper, a sperm-specific calcium channel, plays a crucial role in sperm hyperactivated motility and fertility by mediating Ca influx into sperm. CatSper is the most complicated ion channel known, comprising the pore-forming CATSPER1-4 and multiple auxiliary subunits. However, our previous structural study of mouse CatSper suggests the presence of potential component(s) that remain to be identified. The identity and functional significance of the missing piece(s) of CatSper remain elusive. Here, by combining cryo-EM, mass spectrometry, AlphaFold structure prediction, and coevolutionary analysis, we identify armadillo-like helical domain containing 2 (ARMH2) as a cytosolic component of CatSper. ARMH2 forms a cytosolic ternary subcomplex with EFCAB9 and CATSPERζ, which contributes to the stable assembly of the linear arrangement of CatSper nanodomains along the sperm tail and regulates the pH and Ca sensitivity of the channel. Loss of ARMH2 leads to compromised physiological activation of CatSper, thereby resulting in asthenozoospermia and severe subfertility. These findings show that ARMH2 is crucial for sperm function and provide fresh insights into the composition and functional regulation of CatSper. The integrated methodology employed in identifying ARMH2 also provides valuable approaches for discovering uncharacterized components in other protein complexes.
History
DepositionFeb 15, 2025Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Dec 31, 2025Provider: repository / Type: Initial release
Revision 1.0Dec 31, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Dec 31, 2025Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Dec 31, 2025Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Dec 31, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Dec 31, 2025Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: EF-hand calcium-binding domain-containing protein 9
B: Armadillo-like helical domain containing 2
C: Cation channel sperm-associated auxiliary subunit zeta


Theoretical massNumber of molelcules
Total (without water)76,7273
Polymers76,7273
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein EF-hand calcium-binding domain-containing protein 9


Mass: 26170.482 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Efcab9 / Production host: Mus musculus (house mouse) / References: UniProt: Q9DAM2
#2: Protein Armadillo-like helical domain containing 2


Mass: 27780.201 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Armh2 / Production host: Mus musculus (house mouse) / References: UniProt: A0A286YCZ6
#3: Protein Cation channel sperm-associated auxiliary subunit zeta / CatSper-zeta / CatSperzeta / Protein expressed in male leptotene and zygotene spermatocytes 622 / ...CatSper-zeta / CatSperzeta / Protein expressed in male leptotene and zygotene spermatocytes 622 / MLZ-622 / Testis-expressed protein 40


Mass: 22776.598 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Catsperz, Tex40 / Production host: Mus musculus (house mouse) / References: UniProt: Q9CQP8
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: ARMH2-EFCAB9-CATSPERZ complex / Type: COMPLEX / Entity ID: all / Source: NATURAL
Source (natural)Organism: Mus musculus (house mouse)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1500 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 4.77 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 83920 / Symmetry type: POINT

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