crystal structure of the substrate-binding domain from listeria monocytogenes bile-resistance determinant bile

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ID: 210166
2016
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Abstract
BilE has been reported as a bile resistance determinant that plays an important role in colonization of the gastrointestinal tract by Listeria monocytogenes, the causative agent of listeriosis. The mechanism(s) by which BilE mediates bile resistance are unknown. BilE shares significant sequence similarity with ATP-binding cassette (ABC) importers that contribute to virulence and stress responses by importing quaternary ammonium compounds that act as compatible solutes. Assays using related compounds have failed to demonstrate transport mediated by BilE. The putative substrate-binding domain (SBD) of BilE was expressed in isolation and the crystal structure solved at 1.5 Å. Although the overall fold is characteristic of SBDs, the binding site varies considerably relative to the well-characterized homologs ProX from Archaeoglobus fulgidus and OpuBC and OpuCC from Bacillus subtilis. This suggests that BilE may bind an as-yet unknown ligand. Elucidation of the natural substrate of BilE could reveal a novel bile resistance mechanism.
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ruiz2016crystalscrystal Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Stephanie J. Ruiz;Gea K. Schuurman-Wolters;Bert Poolman
Journal turk kardiyoloji dernegi arsivi
Year 2016
DOI
10.3390/cryst6120162
URL
http://www.mdpi.com/2073-4352/6/12/162
Keywords
listeria monocytogenes abc transporters

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