8SNB
atomic model of sea urchin sperm doublet microtubule (48-nm periodicity)
This is a non-PDB format compatible entry.
Summary for 8SNB
Entry DOI | 10.2210/pdb8snb/pdb |
EMDB information | 40619 40620 40621 |
Descriptor | CFAP96(C4orf47), ATP6V1FNB, Tex26(LOC100888047), ... (58 entities in total) |
Functional Keywords | sperm, doublet microtubule, dmt, microtubule inner protein, cilia, flagella, fap, cfap, mip, map, cytoskeleton, tublin, sea urchin, tex, tektin, saxo, odf, spata, rib, structural protein |
Biological source | Strongylocentrotus purpuratus (purple sea urchin) More |
Total number of polymer chains | 454 |
Total formula weight | 21164642.99 |
Authors | |
Primary citation | Leung, M.R.,Zeng, J.,Wang, X.,Roelofs, M.C.,Huang, W.,Zenezini Chiozzi, R.,Hevler, J.F.,Heck, A.J.R.,Dutcher, S.K.,Brown, A.,Zhang, R.,Zeev-Ben-Mordehai, T. Structural specializations of the sperm tail. Cell, 186:2880-, 2023 Cited by PubMed Abstract: Sperm motility is crucial to reproductive success in sexually reproducing organisms. Impaired sperm movement causes male infertility, which is increasing globally. Sperm are powered by a microtubule-based molecular machine-the axoneme-but it is unclear how axonemal microtubules are ornamented to support motility in diverse fertilization environments. Here, we present high-resolution structures of native axonemal doublet microtubules (DMTs) from sea urchin and bovine sperm, representing external and internal fertilizers. We identify >60 proteins decorating sperm DMTs; at least 15 are sperm associated and 16 are linked to infertility. By comparing DMTs across species and cell types, we define core microtubule inner proteins (MIPs) and analyze evolution of the tektin bundle. We identify conserved axonemal microtubule-associated proteins (MAPs) with unique tubulin-binding modes. Additionally, we identify a testis-specific serine/threonine kinase that links DMTs to outer dense fibers in mammalian sperm. Our study provides structural foundations for understanding sperm evolution, motility, and dysfunction at a molecular level. PubMed: 37327785DOI: 10.1016/j.cell.2023.05.026 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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