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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Oct;69(Pt 10):1182-5. doi: 10.1107/S1744309113024676. Epub 2013 Sep 30.

Purification, crystallization and preliminary crystallographic analysis of the SpaA backbone-pilin subunit from probiotic Lactobacillus rhamnosus GG.

Author information

  • 1Regional Centre for Biotechnology, 180 Udyog Vihar Phase 1, Gurgaon, Haryana 122 016, India.

Abstract

Lactobacillus rhamnosus GG, a widely used Gram-positive probiotic strain, is clinically well known for its perceived health-promoting effects. It has recently been shown to display proteinaceous pilus fibres (called SpaCBA) on its cell surface. Structurally, SpaCBA pili possess a characteristic three-pilin polymerized architecture, with repeating SpaA major pilins that form the backbone and two types of minor subunits (SpaB and SpaC). In this study, recombinant SpaA protein was purified, characterized and crystallized. The crystals diffracted to a resolution of 2.0 Å and belonged to space group C2, with unit-cell parameters a=227.9, b=63.2, c=104.3 Å, β=95.1°.

KEYWORDS:

Lactobacillus rhamnosus GG; SpaCBA pili; adhesion; bacterial surface proteins; fimbria; probiotics; sortase

PMID:
24100577
[PubMed - indexed for MEDLINE]
PMCID:
PMC3792685
[Available on 2015/10/1]
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