Open AccessPurification, crystallization and preliminary crystallographic analysis of Streptococcus pyogenes laminin‐binding protein Lbp
Author(s) -
Linke Christian,
CaradocDavies Tom T.,
Proft Thomas,
Baker Edward N.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108002273
Subject(s) - laminin , streptococcus pyogenes , recombinant dna , adhesion , streptococcus , glycoprotein , bacteria , microbiology and biotechnology , chemistry , crystallography , biology , cell , gene , biochemistry , genetics , organic chemistry , staphylococcus aureus
The laminin‐binding protein Lbp (Spy2007) from Streptococcus pyogenes (a group A streptococcus) mediates adhesion to the human basal lamina glycoprotein laminin. Accordingly, Lbp is essential in in vitro models of cell adhesion and invasion. However, the molecular and structural basis of laminin binding by bacteria remains unknown. Therefore, the lbp gene has been cloned for recombinant expression in Escherichia coli . Lbp has been purified and crystallized from 30%( w / v ) PEG 1500 by the sitting‐drop vapour‐diffusion method. The crystals belonged to the monoclinic space group P 2 1 , with unit‐cell parameters a = 42.62, b = 92.16, c = 70.61 Å, β = 106.27°, and diffracted to 2.5 Å resolution.