8RKG
Crystal structure of tetrameric collagenase-cleaved Xenopus ZP2-N2N3 (cleaved xZP2-N2N3)
This is a non-PDB format compatible entry.
Summary for 8RKG
Entry DOI | 10.2210/pdb8rkg/pdb |
Related | 5BUP 5II6 8RKE 8RKF 8RKH |
EMDB information | 19276 19277 |
Descriptor | XlZPA protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
Functional Keywords | cell adhesion, fertilization, egg-sperm interaction, gamete recognition, sperm receptor, extracellular matrix, egg coat, zona pellucida, glycoprotein, n-glycan, structural protein, zp-n domain, block to polyspermy, post-fertilization cleavage, ovastacin, alphafold |
Biological source | Xenopus laevis (African clawed frog) More |
Total number of polymer chains | 16 |
Total formula weight | 198054.21 |
Authors | Nishio, S.,de Sanctis, D.,Jovine, L. (deposition date: 2023-12-25, release date: 2024-03-13, Last modification date: 2024-11-13) |
Primary citation | Nishio, S.,Emori, C.,Wiseman, B.,Fahrenkamp, D.,Dioguardi, E.,Zamora-Caballero, S.,Bokhove, M.,Han, L.,Stsiapanava, A.,Algarra, B.,Lu, Y.,Kodani, M.,Bainbridge, R.E.,Komondor, K.M.,Carlson, A.E.,Landreh, M.,de Sanctis, D.,Yasumasu, S.,Ikawa, M.,Jovine, L. ZP2 cleavage blocks polyspermy by modulating the architecture of the egg coat. Cell, 187:1440-1459.e24, 2024 Cited by PubMed Abstract: Following the fertilization of an egg by a single sperm, the egg coat or zona pellucida (ZP) hardens and polyspermy is irreversibly blocked. These events are associated with the cleavage of the N-terminal region (NTR) of glycoprotein ZP2, a major subunit of ZP filaments. ZP2 processing is thought to inactivate sperm binding to the ZP, but its molecular consequences and connection with ZP hardening are unknown. Biochemical and structural studies show that cleavage of ZP2 triggers its oligomerization. Moreover, the structure of a native vertebrate egg coat filament, combined with AlphaFold predictions of human ZP polymers, reveals that two protofilaments consisting of type I (ZP3) and type II (ZP1/ZP2/ZP4) components interlock into a left-handed double helix from which the NTRs of type II subunits protrude. Together, these data suggest that oligomerization of cleaved ZP2 NTRs extensively cross-links ZP filaments, rigidifying the egg coat and making it physically impenetrable to sperm. PubMed: 38490181DOI: 10.1016/j.cell.2024.02.013 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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