5MR3
Crystal structure of red abalone egg VERL repeat 2 with linker in complex with sperm lysin at 1.8 A resolution
Summary for 5MR3
| Entry DOI | 10.2210/pdb5mr3/pdb |
| Related | 1LIS 1LYN 2LIS 2LYN 3D4C 3D4G 3EF7 3NK3 3NK4 5II4 5II5 5II7 5II8 5II9 5IIA 5IIB 5IIC 5MR2 |
| Descriptor | Egg-lysin, Vitelline envelope sperm lysin receptor, GLYCEROL, ... (7 entities in total) |
| Functional Keywords | cell adhesion, fertilization, egg-sperm interaction, gamete recognition, sperm receptor, egg coat, vitelline envelope, zp domain, zp-n domain, sperm acrosome, sperm penetration |
| Biological source | Haliotis rufescens (California red abalone) More |
| Cellular location | Cytoplasmic vesicle, secretory vesicle, acrosome lumen : P04552 Cell membrane ; Single-pass membrane protein : Q8WR62 |
| Total number of polymer chains | 8 |
| Total formula weight | 127899.42 |
| Authors | Nishimura, K.,Raj, I.,Sadat Al-Hosseini, H.,De Sanctis, D.,Jovine, L. (deposition date: 2016-12-21, release date: 2017-06-14, Last modification date: 2024-10-16) |
| Primary citation | Raj, I.,Sadat Al Hosseini, H.,Dioguardi, E.,Nishimura, K.,Han, L.,Villa, A.,de Sanctis, D.,Jovine, L. Structural Basis of Egg Coat-Sperm Recognition at Fertilization. Cell, 169:1315-1326.e17, 2017 Cited by PubMed Abstract: Recognition between sperm and the egg surface marks the beginning of life in all sexually reproducing organisms. This fundamental biological event depends on the species-specific interaction between rapidly evolving counterpart molecules on the gametes. We report biochemical, crystallographic, and mutational studies of domain repeats 1-3 of invertebrate egg coat protein VERL and their interaction with cognate sperm protein lysin. VERL repeats fold like the functionally essential N-terminal repeat of mammalian sperm receptor ZP2, whose structure is also described here. Whereas sequence-divergent repeat 1 does not bind lysin, repeat 3 binds it non-species specifically via a high-affinity, largely hydrophobic interface. Due to its intermediate binding affinity, repeat 2 selectively interacts with lysin from the same species. Exposure of a highly positively charged surface of VERL-bound lysin suggests that complex formation both disrupts the organization of egg coat filaments and triggers their electrostatic repulsion, thereby opening a hole for sperm penetration and fusion. PubMed: 28622512DOI: 10.1016/j.cell.2017.05.033 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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