PDBsum entry 4g7e

Hydrolase

PDB id

4g7e

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Contents

			Protein chains

					833 a.a.

			Metals

					_NI ×4


					_MG

			Waters ×656

PDB id:

4g7e

Links

Name:

Hydrolase

Title:

Crystal structure of pigeon pea urease

Structure:

Urease. Chain: a. Urease. Chain: b. Ec: 3.5.1.5

Source:

Cajanus cajan. Pigeon pea. Organism_taxid: 3821. Organism_taxid: 3821

Resolution:

2.20Å

R-factor:

0.220

R-free:

0.268

Authors:

A.Balasubramanian,K.Ponnuraj

Key ref:

A.Balasubramanian et al. (2013). Structural and functional studies on urease from pigeon pea (Cajanus cajan). Int J Biol Macromol, 58, 301-309. PubMed id: 23624166 DOI: 10.1016/j.ijbiomac.2013.04.055

Date:

20-Jul-12

Release date:

05-Jun-13

PROCHECK

	Headers

	References

Protein chains

I3PA93 (I3PA93_CAJCA) - Urease from Cajanus cajan

Seq: Struc:

Seq: Struc:					838 a.a. 833 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 65 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

E.C.3.5.1.5 - urease.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

urea + 2 H2O + H⁺ = hydrogencarbonate + 2 NH4⁺

urea	+	2 × H2O	+	H(+)	=	hydrogencarbonate	+	2 × NH4(+)

Cofactor:

Ni(2+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1016/j.ijbiomac.2013.04.055	Int J Biol Macromol 58:301-309 (2013)
PubMed id: 23624166

Structural and functional studies on urease from pigeon pea (Cajanus cajan).
A.Balasubramanian, V.Durairajpandian, S.Elumalai, N.Mathivanan, A.K.Munirajan, K.Ponnuraj.

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.