Next Article in Journal
Development of 20 Microsatellite Markers for Solenocera crassicornis and Their Cross-Species Application in Solenocera melantho
Next Article in Special Issue
Correlation between Protein Sequence Similarity and Crystallization Reagents in the Biological Macromolecule Crystallization Database
Previous Article in Journal
Antioxidative Properties of Crude Polysaccharides from Inonotus obliquus
Previous Article in Special Issue
Structural Analysis of Cytochrome P450 105N1 Involved in the Biosynthesis of the Zincophore, Coelibactin
Int. J. Mol. Sci. 2012, 13(7), 9207-9217; doi:10.3390/ijms13079207

3D Structure Elucidation of Thermostable L2 Lipase from Thermophilic Bacillus sp. L2

1,2,* , 1
Received: 16 May 2012 / Revised: 29 June 2012 / Accepted: 12 July 2012 / Published: 23 July 2012
(This article belongs to the Special Issue Protein Crystallography in Molecular Biology)
View Full-Text   |   Download PDF [1776 KB, uploaded 19 June 2014]   |   Browse Figures


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 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.
Keywords: thermostable lipase; L2 lipase; crystallization; counterdiffusion; crystal structure thermostable lipase; L2 lipase; crystallization; counterdiffusion; crystal structure
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Share & Cite This Article

Further Mendeley | CiteULike
Export to BibTeX |
MDPI and ACS Style

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

Related Articles

Article Metrics

For more information on the journal, click here


Cited By

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert