ArticleThe Biochemical journal2009
Identification and characterization of the lipid-binding property of GrlR, a locus of enterocyte effacement regulator.
Article in The Biochemical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Genomic analysis of shiga toxin-containing Escherichia coli O157:H7 isolated from Argentinean cattle.PloS one · 2021Article
- TheProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Advances on the Transfer of Lipids by Lipid Transfer Proteins.Trends in biochemical sciences · 2017Review
- Article
- Bacterial Thymidylate Synthase Binds Two Molecules of Substrate and Cofactor without Cooperativity.Journal of the American Chemical Society · 2015Article
- Latest developments in experimental and computational approaches to characterize protein-lipid interactions.Proteomics · 2012Review
- Article
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Authors and funding
7 authors.
Funding
Abstract
Lipocalins are a broad family of proteins identified initially in eukaryotes and more recently in Gram-negative bacteria. The functions of lipocalin or lipid-binding proteins are often elusive and very diverse. Recently, we have determined the structure of GrlR (global regulator of LEE repressor), which plays a key role in the regulation of LEE (locus of enterocyte effacement) proteins. GrlR adopts a lipocalin-like fold that is composed of an eight-stranded beta-barrel followed by an alpha-helix at the C-terminus. GrlR has a highly hydrophobic cavity region and could be a potential transporter of lipophilic molecules. To verify this hypothesis, we carried out structure-based analysis of GrlR, determined the structure of the lipid-GrlR complex and measured the binding of lipid to recombinant GrlR by ITC (isothermal titration calorimetry). In addition, we identified phosphatidylglycerol and phosphatidylethanolamine as the endogenously bound lipid species of GrlR using electrospray-ionization MS. Furthermore, we have shown that the lipid-binding property of GrlR is similar to that of its closest lipocalin structural homologue, beta-lactoglobulin. Our studies demonstrate the hitherto unknown lipid-binding property of GrlR.
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