4G7E

Crystal structure of pigeon pea urease

Summary for 4G7E

• Entry DOI: 10.2210/pdb4g7e/pdb
• Descriptor: urease, NICKEL (II) ION, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: urease, pigeon pea, tim barrel domain, b domain, catalyzes urea hydrolysis to ammonia, carbon di-oxide, hydrolase
• Biological source: Cajanus cajan (pigeon pea); More
• Total number of polymer chains: 2
• Total formula weight: 180410.19

Authors

Balasubramanian, A.,Ponnuraj, K. (deposition date: 2012-07-20, release date: 2013-06-05, Last modification date: 2025-03-26)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)