ArticleFEBS letters2006
The membrane bound bacterial lipocalin Blc is a functional dimer with binding preference for lysophospholipids.
Article in FEBS letters, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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25 citing papers in PubMed, 61 citations in OpenAlex.
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- Serotype-dependent adhesion of Shiga toxin-producingFrontiers in microbiology · 2022Article
- Cell Envelope Stress Response in Pseudomonas aeruginosa.Advances in experimental medicine and biology · 2022Article
- Computational redesign of a fluorogen activating protein with Rosetta.PLoS computational biology · 2021Article
- Lipocalin Blc is a potential heme-binding protein.FEBS letters · 2021Article
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- A lipocalin mediates unidirectional heme biomineralization in malaria parasites.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- DiB-splits: nature-guided design of a novel fluorescent labeling split system.Scientific reports · 2020Article
- A SNP of bacterial blc disturbs gut lysophospholipid homeostasis and induces inflammation through epithelial barrier disruption.EBioMedicine · 2020Article
- The Lipoprotein NlpE Is a Cpx Sensor That Serves as a Sentinel for Protein Sorting and Folding Defects in theJournal of bacteriology · 2019Article
- Stress-induced lipocalin-2 controls dendritic spine formation and neuronal activity in the amygdala.PloS one · 2013Article
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- Structure of the first representative of Pfam family PF09410 (DUF2006) reveals a structural signature of the calycin superfamily that suggests a role in lipid metabolism.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Mutation analysis of violaxanthin de-epoxidase identifies substrate-binding sites and residues involved in catalysis.The Journal of biological chemistry · 2010Article
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
Abstract
Lipocalins, a widespread multifunctional family of small proteins (15-25kDa) have been first described in eukaryotes and more recently in Gram-negative bacteria. Bacterial lipocalins belonging to class I are outer membrane lipoproteins, among which Blc from E. coli is the better studied. Blc is expressed under conditions of starvation and high osmolarity, conditions known to exert stress on the cell envelope. The structure of Blc that we have previously solved (V. Campanacci, D. Nurizzo, S. Spinelli, C. Valencia, M. Tegoni, C. Cambillau, FEBS Lett. 562 (2004) 183-188.) suggested its possible role in binding fatty acids or phospholipids. Both physiological and structural data on Blc, therefore, point to a role in storage or transport of lipids necessary for membrane maintenance. In order to further document this hypothesis for Blc function, we have performed binding studies using fluorescence quenching experiments. Our results indicate that dimeric Blc binds fatty acids and phospholipids in a micromolar K(d) range. The crystal structure of Blc with vaccenic acid, an unsaturated C18 fatty acid, reveals that the binding site spans across the Blc dimer, opposite to its membrane anchored face. An exposed unfilled pocket seemingly suited to bind a polar group attached to the fatty acid prompted us to investigate lyso-phospholipids, which were found to bind in a nanomolar K(d) range. We discuss these findings in terms of a potential role for Blc in the metabolism of lysophospholipids generated in the bacterial outer membrane.
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