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-Structure paper
タイトル | Structure of a mammalian sperm cation channel complex. |
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ジャーナル・号・ページ | Nature, Vol. 595, Issue 7869, Page 746-750, Year 2021 |
掲載日 | 2021年7月5日 |
著者 | Shiyi Lin / Meng Ke / Yuqi Zhang / Zhen Yan / Jianping Wu / |
PubMed 要旨 | The cation channel of sperm (CatSper) is essential for sperm motility and fertility. CatSper comprises the pore-forming proteins CATSPER1-4 and multiple auxiliary subunits, including CATSPERβ, γ, ...The cation channel of sperm (CatSper) is essential for sperm motility and fertility. CatSper comprises the pore-forming proteins CATSPER1-4 and multiple auxiliary subunits, including CATSPERβ, γ, δ, ε, ζ, and EFCAB9. Here we report the cryo-electron microscopy (cryo-EM) structure of the CatSper complex isolated from mouse sperm. In the extracellular view, CATSPER1-4 conform to the conventional domain-swapped voltage-gated ion channel fold, following a counterclockwise arrangement. The auxiliary subunits CATSPERβ, γ, δ and ε-each of which contains a single transmembrane segment and a large extracellular domain-constitute a pavilion-like structure that stabilizes the entire complex through interactions with CATSPER4, 1, 3 and 2, respectively. Our EM map reveals several previously uncharacterized components, exemplified by the organic anion transporter SLCO6C1. We name this channel-transporter ultracomplex the CatSpermasome. The assembly and organization details of the CatSpermasome presented here lay the foundation for the development of CatSpermasome-related treatments for male infertility and non-hormonal contraceptives. |
リンク | Nature / PubMed:34225353 |
手法 | EM (単粒子) |
解像度 | 2.9 Å |
構造データ | EMDB-31076, PDB-7eeb: |
化合物 | ChemComp-NA: ChemComp-9Z9: ChemComp-NAG: |
由来 |
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キーワード | PROTEIN TRANSPORT / ion channel / membrane protein / calcium channel / protein complex |