publication . Article . 2016

Crystal Structure of the Substrate-Binding Domain from Listeria monocytogenes Bile-Resistance Determinant BilE

Stephanie J Ruiz; Gea K. Schuurman-Wolters; Bert Poolman;
Open Access English
  • Published: 01 Dec 2016 Journal: Crystals, volume 6, issue 12, page 162 (eissn: 2073-4352, Copyright policy)
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 solve...
Medical Subject Headings: digestive system
free text keywords: Listeria monocytogenes, ABC transporters, ABC importers, substrate-binding protein, substrate-binding domain, bile resistance, lmo1421, lmo1422, SOLUTES GLYCINE BETAINE, ABC TRANSPORTER, BACILLUS-SUBTILIS, COMPATIBLE SOLUTES, LIGAND-BINDING, GASTROINTESTINAL PERSISTENCE, LACTOCOCCUS-LACTIS, ESCHERICHIA-COLI, PROLINE BETAINE, PROTEIN OPUAC, Inorganic Chemistry, General Materials Science, General Chemical Engineering, Condensed Matter Physics, lcsh:Crystallography, lcsh:QD901-999, Biochemistry, Bacillus subtilis, biology.organism_classification, biology, ATP-binding cassette transporter, Escherichia coli, medicine.disease_cause, medicine, Virulence, CYP8B1, Materials science, Ligand (biochemistry), Binding site
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Funded by
EC| ABCvolume
The ABC of Cell Volume Regulation
  • Funder: European Commission (EC)
  • Project Code: 670578
  • Funding stream: H2020 | ERC | ERC-ADG
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Article . 2016
Article . 2016
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