Open AccessCrystallization and preliminary crystallographic studies of LipA, a secretory lipase/esterase from Xanthomonas oryzae pv. oryzae
Author(s) -
Aparna Gudlur,
Chatterjee Avradip,
Jha Gopaljee,
Sonti Ramesh V.,
Sankaranarayanan Rajan
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107034367
Subject(s) - lipase , xanthomonas oryzae , crystallization , xanthomonas oryzae pv. oryzae , esterase , crystallography , chemistry , microbiology and biotechnology , biology , materials science , enzyme , biochemistry , organic chemistry , pathogen
Xanthomonas oryzae pv. oryzae is the causal agent of bacterial leaf blight, a serious disease of rice. Several enzymes that are secreted through the type II secretion system of this bacterium play an important role in the plant–microbe interaction, being important for virulence and also being able to induce potent host defence responses. One of these enzymes is a secretory lipase/esterase, LipA, which shows a very weak homology to other bacterial lipases and gives a positive tributyrin plate assay. In this study, LipA was purified from the culture supernatant of an overexpressing clone of X. oryzae pv. oryzae and two types of crystals belonging to space group C 2 but with two different unit‐cell parameters were obtained using the hanging‐drop vapour‐diffusion method. Type I crystals diffract to a maximum resolution of 1.89 Å and have unit‐cell parameters a = 93.1, b = 62.3, c = 66.1 Å, β = 90.8°. Type II crystals have unit‐cell parameters a = 103.6, b = 54.6, c = 66.3 Å, β = 92.6° and diffract to 1.86 Å. Solvent‐content analysis shows one monomer in the asymmetric unit in both the crystal forms.