4FDM: Crystallization And 3d Structure Elucidation Of Thermostable L2 Lipase From Thermophilic Locally Isolated Bacillus Sp. L2

Citation:
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 x 0.1 x 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 A 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 A, alpha = beta = gamma = 90 degrees . 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 A Da(-1). The 3D structure of L2 lipase revealed topological organization of alpha/beta-hydrolase fold consisting of 11 beta-strands and 13 alpha-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.
PDB ID: 4FDMDownload
MMDB ID: 109840
PDB Deposition Date: 2012/5/29
Updated in MMDB: 2013/05
Experimental Method:
x-ray diffraction
Resolution: 1.6  Å
Source Organism:
Similar Structures:
Biological Unit for 4FDM: monomeric; determined by author and by software (PISA)
Molecular Components in 4FDM
Label Count Molecule
Protein (1 molecule)
1
Thermostable Lipase
Molecule annotation
Chemicals (2 molecules)
1
1
2
1
* Click molecule labels to explore molecular sequence information.

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