2LIS

HIGH RESOLUTION STRUCTURE OF THE RED ABALONE LYSIN MONOMER

2LIS の概要

• エントリーDOI: 10.2210/pdb2lis/pdb
• 関連するPDBエントリー: 2LYN
• 分子名称: SPERM LYSIN (2 entities in total)
• 機能のキーワード: abalone lysin, fertilization protein, gamete recognition protein, cell adhesion
• 由来する生物種: Haliotis rufescens (California red abalone)
• 細胞内の位置: Cytoplasmic vesicle, secretory vesicle, acrosome lumen : P04552
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16295.22

構造登録者

Kresge, N.,Vacquier, V.D.,Stout, C.D. (登録日: 1999-04-16, 公開日: 2000-01-21, 最終更新日: 2023-12-27)

主引用文献

Kresge, N.,Vacquier, V.D.,Stout, C.D.
1.35 and 2.07 A resolution structures of the red abalone sperm lysin monomer and dimer reveal features involved in receptor binding.
Acta Crystallogr.,Sect.D, 56:34-41, 2000

PubMed Abstract: Abalone sperm use lysin to make a hole in the egg's protective vitelline envelope (VE). When released from sperm, lysin first binds to the VE receptor for lysin (VERL) then dissolves the VE by a non-enzymatic mechanism. The structures of the monomeric and dimeric forms of Haliotis rufescens (red abalone) lysin, previously solved at 1.90 and 2.75 A, respectively, have now been refined to 1.35 and 2.07 A, respectively. The monomeric form of lysin was refined using previously obtained crystallization conditions, while the dimer was solved in a new crystal form with four molecules (two dimers) per asymmetric unit. These high-resolution structures reveal alternate residue conformations, enabling a thorough analysis of the conserved residues contributing to the amphipathic nature of lysin. The availability of five independent high-resolution copies of lysin permits comparisons leading to insights on the local flexibility of lysin and alternative conformations of the hypervariable N-terminus, thought to be involved in species-specific receptor recognition. The new analysis led to the discovery of the basic nature of a cleft formed upon dimerization and a patch of basic residues in the dimer interface. Identification of these features was not possible at lower resolution. In light of this new information, a model explaining the binding of sperm lysin to egg VERL and the subsequent dissolution of the egg VE is proposed.

PubMed: 10666624
DOI: 10.1107/S0907444999014626

実験手法

X-RAY DIFFRACTION (1.35 Å)