4G7E

Crystal structure of pigeon pea urease

4G7E の概要

• エントリーDOI: 10.2210/pdb4g7e/pdb
• 分子名称: urease, NICKEL (II) ION, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: urease, pigeon pea, tim barrel domain, b domain, catalyzes urea hydrolysis to ammonia, carbon di-oxide, hydrolase
• 由来する生物種: Cajanus cajan (pigeon pea); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 180410.19

構造登録者

Balasubramanian, A.,Ponnuraj, K. (登録日: 2012-07-20, 公開日: 2013-06-05, 最終更新日: 2025-03-26)

主引用文献

Balasubramanian, A.,Durairajpandian, V.,Elumalai, S.,Mathivanan, N.,Munirajan, A.K.,Ponnuraj, K.
Structural and functional studies on urease from pigeon pea (Cajanus cajan)
Int.J.Biol.Macromol., 58C:301-309, 2013

PubMed Abstract: Urease is an enzyme that catalyzes the hydrolysis of urea, forming ammonia and carbon dioxide, and is found in plants, microorganisms and invertebrates. Although plant and bacterial ureases are closely related at amino acid and at the structural level, the insecticidal activity is seen only in the plant ureases. In contrast, both plant and bacterial ureases exhibit antifungal activity. These two biological properties are independent of its ureolytic activity. However, till date the mechanism(s) behind the insecticidal and fungicidal activity of ureases are not clearly understood. Here we report the crystal structure of pigeon pea urease (PPU, Cajanus cajan) which is the second structure from the plant source. We have deduced the amino acid sequence of PPU and also report here studies on its stability, insecticidal and antifungal activity. PPU exhibits cellulase activity. Based on the structural analysis of PPU and docking studies with cellopentoase we propose a possible mechanism of antifungal activity of urease.

PubMed: 23624166
DOI: 10.1016/j.ijbiomac.2013.04.055

実験手法

X-RAY DIFFRACTION (2.2 Å)