1NPC

THE STRUCTURE OF NEUTRAL PROTEASE FROM BACILLUS CEREUS AT 0.2-NM RESOLUTION

1NPC の概要

• エントリーDOI: 10.2210/pdb1npc/pdb
• 分子名称: NEUTRAL PROTEASE, CALCIUM ION, ZINC ION, ... (4 entities in total)
• 機能のキーワード: hydrolase(metalloproteinase)
• 由来する生物種: Bacillus cereus
• 細胞内の位置: Secreted: P05806
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34042.22

構造登録者

Stark, W.,Pauptit, R.A.,Jansonius, J.N. (登録日: 1992-01-08, 公開日: 1993-10-31, 最終更新日: 2024-02-14)

主引用文献

Stark, W.,Pauptit, R.A.,Wilson, K.S.,Jansonius, J.N.
The structure of neutral protease from Bacillus cereus at 0.2-nm resolution.
Eur.J.Biochem., 207:781-791, 1992

PubMed Abstract: The crystal structure of the neutral protease from Bacillus cereus has been refined to an R factor of 17.5% at 0.2-nm resolution. The enzyme, an extracellular metalloendopeptidase, consists of two domains and binds one zinc and four calcium ions. The structure is very similar to that of thermolysin, with which the enzyme shares 73% amino-acid sequence identity. The active-site cleft between the two domains is wider in neutral protease than in thermolysin. This suggests the presence of a flexible hinge region between the two domains, which may assist enzyme action. The high-resolution analysis allows detailed examination of possible causes for the difference in thermostability between neutral protease and thermolysin.

PubMed: 1633827
DOI: 10.1111/j.1432-1033.1992.tb17109.x

実験手法

X-RAY DIFFRACTION (2 Å)