5IIB

Crystal structure of red abalone egg VERL repeat 3 in complex with sperm lysin at 1.64 A resolution (crystal form II)

5IIB の概要

• エントリーDOI: 10.2210/pdb5iib/pdb
• 関連するPDBエントリー: 1LIS 1LYN 2LIS 2LYN 3D4C 3D4G 3EF7 3NK3 3NK4 5II4 5II5 5II7 5II8 5II9 5IIA 5IIC
• 関連するBIRD辞書のPRD_ID: PRD_900003
• 分子名称: Egg-lysin, Vitelline envelope sperm lysin receptor, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: cell adhesion, fertilization, egg-sperm interaction, gamete recognition, sperm receptor, egg coat, vitelline envelope, zp domain, zp-n domain, sperm acrosome, egg coat penetration
• 由来する生物種: Haliotis rufescens (California red abalone); 詳細
• 細胞内の位置: Cytoplasmic vesicle, secretory vesicle, acrosome lumen : P04552; Cell membrane ; Single-pass membrane protein : Q8WR62
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31750.62

構造登録者

Raj, I.,Sadat Al-Hosseini, H.,Nishimura, K.,De Sanctis, D.,Jovine, L. (登録日: 2016-03-01, 公開日: 2017-06-14, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.64 Å)