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3D Structure Elucidation of Thermostable L2 Lipase from Thermophilic Bacillus sp. L2
AbstractThe crystallization of proteins makes it possible to determine their structure by X-ray crystallography, and is therefore important for the analysis of protein structure-function relationships. L2 lipase was crystallized by using the J-tube counter diffusion method. A crystallization consisting of 20% PEG 6000, 50 mM MES pH 6.5 and 50 mM NaCl was found to be the best condition to produce crystals with good shape and size (0.5 × 0.1 × 0.2 mm). The protein concentration used for the crystallization was 3 mg/mL. L2 lipase crystal has two crystal forms, Shape 1 and Shape 2. Shape 2 L2 lipase crystal was diffracted at 1.5 Å and the crystal belongs to the orthorhombic space group P212121, with unit-cell parameters a = 72.0, b = 81.8, c = 83.4 Å, α = β = γ = 90°. There is one molecule per asymmetric unit and the solvent content of the crystals is 56.9%, with a Matthew’s coefficient of 2.85 Å Da−1. The 3D structure of L2 lipase revealed topological organization of α/β-hydrolase fold consisting of 11 β-strands and 13 α-helices. Ser-113, His-358 and Asp-317 were assigned as catalytic triad residues. One Ca2+ and one Zn2+ were found in the L2 lipase molecule.
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Raja Abd. Rahman, R.N.Z.; Mohd Shariff, F.; Basri, M.; Salleh, A.B. 3D Structure Elucidation of Thermostable L2 Lipase from Thermophilic Bacillus sp. L2. Int. J. Mol. Sci. 2012, 13, 9207-9217.View more citation formats
Raja Abd. Rahman RNZ, Mohd Shariff F, Basri M, Salleh AB. 3D Structure Elucidation of Thermostable L2 Lipase from Thermophilic Bacillus sp. L2. International Journal of Molecular Sciences. 2012; 13(7):9207-9217.Chicago/Turabian Style
Raja Abd. Rahman, Raja Noor Zaliha; Mohd Shariff, Fairolniza; Basri, Mahiran; Salleh, Abu Bakar. 2012. "3D Structure Elucidation of Thermostable L2 Lipase from Thermophilic Bacillus sp. L2." Int. J. Mol. Sci. 13, no. 7: 9207-9217.