Purification, crystallization and preliminary crystallographic analysis of Streptococcus pyogenes laminin-binding protein Lbp.
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 P2(1), with unit-cell parameters a = 42.62, b = 92.16, c = 70.61 A, beta = 106.27 degrees, and diffracted to 2.5 A resolution.
Linke
Christian
C
School of Biological Sciences, University of Auckland, Private Bag 92019, Auckland, New Zealand. clin180@ec.auckland.ac.nz
Caradoc-Davies
Tom T
TT
Proft
Thomas
T
Baker
Edward N
EN
D001483:Base Sequence; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D017931:DNA Primers; D007797:Laminin / Q000378:metabolism*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013297:Streptococcus pyogenes / Q000737:chemistry*
D002352:Carrier Proteins; D017931:DNA Primers; D007797:Laminin; D011994:Recombinant Proteins