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Purification, crystallization and preliminary crystallographic analysis of Streptococcus pyogenes laminin-binding protein Lbp.

ABSTRACT: 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.

SUBMITTER: Linke C

PROVIDER: S-EPMC2374178 | biostudies-literature | 2008 Feb

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary crystallographic analysis of Streptococcus pyogenes laminin-binding protein Lbp.

Linke Christian C Caradoc-Davies Tom T TT Proft Thomas T Baker Edward N EN

Acta crystallographica. Section F, Structural biology and crystallization communications 20080131 Pt 2

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-d ...[more]

PMID: 18259070

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