1WQS

Crystal structure of Norovirus 3C-like protease

1WQS の概要

• エントリーDOI: 10.2210/pdb1wqs/pdb
• 分子名称: 3C-like protease, MERCURY (II) ION, L(+)-TARTARIC ACID, ... (5 entities in total)
• 機能のキーワード: norovirus, 3c-like protease, chymotrypsin like protease, oxyanion hole, norwalk-like virus, hydrolase
• 由来する生物種: Chiba virus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 76226.96

構造登録者

Nakamura, K.,Someya, Y.,Kumasaka, T.,Tanaka, N. (登録日: 2004-10-01, 公開日: 2005-10-04, 最終更新日: 2024-12-25)

主引用文献

Nakamura, K.,Someya, Y.,Kumasaka, T.,Ueno, G.,Yamamoto, M.,Sato, T.,Takeda, N.,Miyamura, T.,Tanaka, N.
A norovirus protease structure provides insights into active and substrate binding site integrity
J.Virol., 79:13685-13693, 2005

PubMed Abstract: Norovirus 3C-like proteases are crucial to proteolytic processing of norovirus polyproteins. We determined the crystal structure of the 3C-like protease from Chiba virus, a norovirus, at 2.8-A resolution. An active site including Cys139 and His30 is present, as is a hydrogen bond network that stabilizes the active site conformation. In the oxyanion hole backbone, a structural difference was observed probably upon substrate binding. A peptide substrate/enzyme model shows that several interactions between the two components are critical for substrate binding and that the S1 and S2 sites appropriately accommodate the substrate P1 and P2 residues, respectively. Knowledge of the structure and a previous mutagenesis study allow us to correlate proteolysis and structure.

PubMed: 16227288
DOI: 10.1128/JVI.79.21.13685-13693.2005

実験手法

X-RAY DIFFRACTION (2.8 Å)