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

被引：4

作者：

Linke, Christian ^{[1
]}

Caradoc-Davies, Tom T. ^{[1
,2
]}

Proft, Thomas ^{[3
]}

Baker, Edward N. ^{[1
]}

机构：

[1] Univ Auckland, Sch Biol Sci, Auckland 1, New Zealand

[2] Australian Synchrotron, Clayton, Vic 3168, Australia

[3] Univ Auckland, Sch Med Sci, Auckland 1, New Zealand

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2008年 / 64卷

关键词：

D O I：

10.1107/S1744309108002273

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 angstrom, beta = 106.27 degrees, and diffracted to 2.5 angstrom resolution.

引用

页码：141 / 143

页数：3

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