4g7e

Crystal structure of pigeon pea urease

spinqualitylabelsall models 4g7e, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4g7e is a 2 chain structure with sequence from Cajanus cajan. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: CME, KCX, MG, NI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function I3PA93_CAJCA Publication Abstract from PubMed 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. Structural and functional studies on urease from pigeon pea (Cajanus cajan).,Balasubramanian A, Durairajpandian V, Elumalai S, Mathivanan N, Munirajan AK, Ponnuraj K Int J Biol Macromol. 2013 Jul;58:301-9. doi: 10.1016/j.ijbiomac.2013.04.055. Epub, 2013 Apr 24. PMID:23624166 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Urease 3D structures

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