4FDM
Crystallization and 3D structure elucidation of thermostable L2 lipase from thermophilic locally isolated Bacillus sp. L2.
Summary for 4FDM
| Entry DOI | 10.2210/pdb4fdm/pdb |
| Descriptor | Thermostable lipase, ZINC ION, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | thermostable lipase, hydrolase |
| Biological source | Bacillus sp. L2 |
| Total number of polymer chains | 1 |
| Total formula weight | 44179.54 |
| Authors | Rahman, R.N.Z.R.A.,Shariff, F.M.,Salleh, A.B.,Basri, M.B. (deposition date: 2012-05-29, release date: 2013-05-08, Last modification date: 2023-09-13) |
| Primary citation | Abd Rahman, R.N.,Shariff, F.M.,Basri, M.,Salleh, A.B. 3D Structure Elucidation of Thermostable L2 Lipase from Thermophilic Bacillus sp. L2. Int.J.Mol.Sci., 13:9207-9217, 2012 Cited by PubMed Abstract: The 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 P2(1)2(1)2(1), 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 Ca(2+) and one Zn(2+) were found in the L2 lipase molecule. PubMed: 22942761DOI: 10.3390/ijms13079207 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
Download full validation report
