5II5

Crystal structure of red abalone VERL repeat 1 at 1.8 A resolution

Summary for 5II5

• Entry DOI: 10.2210/pdb5ii5/pdb
• Related: 3D4C 3D4G 3EF7 3NK3 3NK4 5II4 5II6 5IIA 5IIB 5IIC
• Related PRD ID: PRD_900001
• Descriptor: Maltose-binding periplasmic protein,Vitelline envelope sperm lysin receptor, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, TRIETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: cell adhesion, fertilization, egg-sperm interaction, gamete recognition, vitelline envelope, sperm receptor
• Biological source: Escherichia coli; More
• Total number of polymer chains: 1
• Total formula weight: 55414.53

Authors

Sadat Al-Hosseini, H.,Raj, I.,Nishimura, K.,Jovine, L. (deposition date: 2016-03-01, release date: 2017-06-14, Last modification date: 2024-11-13)

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

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: 28622512
DOI: 10.1016/j.cell.2017.05.033

Experimental method

X-RAY DIFFRACTION (1.8 Å)