3LQB

Crystal structure of the hatching enzyme ZHE1 from the zebrafish Danio rerio

3LQB の概要

• エントリーDOI: 10.2210/pdb3lqb/pdb
• 分子名称: LOC792177 protein, SULFATE ION, ZINC ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, metalloprotease, hatching enzyme, astacin, metal-binding, protease
• 由来する生物種: Danio rerio (zebrafish)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22698.91

構造登録者

Tanokura, M.,Okada, A.,Nagata, K.,Yasumasu, S.,Ohtsuka, J.,Iuchi, I. (登録日: 2010-02-08, 公開日: 2010-09-08, 最終更新日: 2024-10-30)

主引用文献

Okada, A.,Sano, K.,Nagata, K.,Yasumasu, S.,Ohtsuka, J.,Yamamura, A.,Kubota, K.,Iuchi, I.,Tanokura, M.
Crystal structure of zebrafish hatching enzyme 1 from the zebrafish Danio rerio
J.Mol.Biol., 402:865-878, 2010

PubMed Abstract: Fish hatching enzymes are zinc metalloproteases that digest the egg envelope (chorion) at the time of hatching. The crystal structure of zebrafish hatching enzyme 1 (ZHE1) has been solved at 1.10 Å resolution. ZHE1 is monomeric, is mitten shaped, and has a cleft at the center of the molecule. ZHE1 consists of three 3(10)-helices, three α-helices, and two β-sheets. The central cleft represents the active site of the enzyme that is crucial for substrate recognition and catalysis. Alanine-scanning mutagenesis of the two substrate peptides has shown that AspP1' contributes the most and that the residues at P4-P2' also contribute to the recognition of the major substrate peptide by ZHE1, whereas GluP3' and the hydrophobic residues at P4-P2, P2', and P5' contribute significantly to the recognition of the minor substrate peptide by ZHE1. Molecular models of these two substrate peptides bound to ZHE1 have been built based on the crystal structure of a transition-state analog inhibitor bound to astacin. In substrate-recognition models, the AspP1' in the major substrate peptide forms a salt bridge with Arg182 of ZHE1, while the GluP3' in the minor substrate peptide instead forms a salt bridge with Arg182. Thus, these two substrate peptides would be differently recognized by ZHE1. The shapes and electrostatic potentials of the substrate-binding clefts of ZHE1 and the structurally similar proteins astacin and bone morphogenetic protein 1 are significantly dissimilar due to different side chains, which would confer their distinctive substrate preferences.

PubMed: 20727360
DOI: 10.1016/j.jmb.2010.08.023

実験手法

X-RAY DIFFRACTION (1.1 Å)