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TitleStructure of a mammalian sperm cation channel complex.
Journal, issue, pagesNature, Vol. 595, Issue 7869, Page 746-750, Year 2021
Publish dateJul 5, 2021
AuthorsShiyi Lin / Meng Ke / Yuqi Zhang / Zhen Yan / Jianping Wu /
PubMed AbstractThe 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.
External linksNature / PubMed:34225353
MethodsEM (single particle)
Resolution2.9 Å
Structure data

31076

7eeb

EMDB-31076, PDB-7eeb:
Structure of the CatSpermasome
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-9Z9:
(3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en / detergent*YM

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • mus musculus (house mouse)
  • human cytomegalovirus
KeywordsPROTEIN TRANSPORT / ion channel / membrane protein / calcium channel / protein complex

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