Publication Date:
2013-03-28
Description:
Serine glutamate repeat A (SgrA) protein is an LPxTG surface adhesin ofEnterococcus faeciumand is the first bacterial nidogen-binding protein identified to date. It has been suggested that it binds to human nidogen, the extracellular matrix molecule of basal lamina, and plays a key role in the invasion and colonization of eukaryotic host cells. SgrA28–288, having both a putative ligand-binding A domain and repetitive B domain, was expressed inEscherichia coliand purified using Ni-affinity and hydrophobic interaction chromatography. Further, the putative ligand-binding region, rSgrA28–153, was subcloned, overexpressed and purified in both native and selenomethionine-derivative forms. The native rSgrA28–153protein crystallized in the monoclinic space groupP21and diffracted to 3.3 Å resolution using an in-house X-ray source, with unit-cell parametersa= 35.84,b= 56.35,c= 60.20 Å, β = 106.5°.
Print ISSN:
1744-3091
Topics:
Biology
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Chemistry and Pharmacology
,
Geosciences
,
Physics
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