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3D structure elucidation of thermostable L2 lipase from thermophilic Bacillus sp. L2

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 2...

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Main Authors: Raja Abdul Rahman, Raja Noor Zaliha, Mohd Shariff, Fairolniza, Basri, Mahiran, Salleh, Abu Bakar
Format: Article
Language:English
Published: MDPI 2012
Online Access:http://psasir.upm.edu.my/id/eprint/77976/1/77976.pdf
http://psasir.upm.edu.my/id/eprint/77976/
https://www.mdpi.com/1422-0067/13/7/9207
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spelling my.upm.eprints.779762020-06-01T03:00:55Z http://psasir.upm.edu.my/id/eprint/77976/ 3D structure elucidation of thermostable L2 lipase from thermophilic Bacillus sp. L2 Raja Abdul Rahman, Raja Noor Zaliha Mohd Shariff, Fairolniza Basri, Mahiran Salleh, Abu Bakar 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. MDPI 2012 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/77976/1/77976.pdf Raja Abdul Rahman, Raja Noor Zaliha and Mohd Shariff, Fairolniza and Basri, Mahiran and Salleh, Abu Bakar (2012) 3D structure elucidation of thermostable L2 lipase from thermophilic Bacillus sp. L2. International Journal of Molecular Sciences, 13 (7). pp. 9207-9217. ISSN 1661-6596; ESSN: 1422-0067 https://www.mdpi.com/1422-0067/13/7/9207 10.3390/ijms13079207
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
language English
description 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.
format Article
author Raja Abdul Rahman, Raja Noor Zaliha
Mohd Shariff, Fairolniza
Basri, Mahiran
Salleh, Abu Bakar
spellingShingle Raja Abdul Rahman, Raja Noor Zaliha
Mohd Shariff, Fairolniza
Basri, Mahiran
Salleh, Abu Bakar
3D structure elucidation of thermostable L2 lipase from thermophilic Bacillus sp. L2
author_facet Raja Abdul Rahman, Raja Noor Zaliha
Mohd Shariff, Fairolniza
Basri, Mahiran
Salleh, Abu Bakar
author_sort Raja Abdul Rahman, Raja Noor Zaliha
title 3D structure elucidation of thermostable L2 lipase from thermophilic Bacillus sp. L2
title_short 3D structure elucidation of thermostable L2 lipase from thermophilic Bacillus sp. L2
title_full 3D structure elucidation of thermostable L2 lipase from thermophilic Bacillus sp. L2
title_fullStr 3D structure elucidation of thermostable L2 lipase from thermophilic Bacillus sp. L2
title_full_unstemmed 3D structure elucidation of thermostable L2 lipase from thermophilic Bacillus sp. L2
title_sort 3d structure elucidation of thermostable l2 lipase from thermophilic bacillus sp. l2
publisher MDPI
publishDate 2012
url http://psasir.upm.edu.my/id/eprint/77976/1/77976.pdf
http://psasir.upm.edu.my/id/eprint/77976/
https://www.mdpi.com/1422-0067/13/7/9207
_version_ 1669008847004499968
score 13.211869

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