Structural highlights
Function
BLC_ECOLI Involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Displays a binding preference for lysophospholipids.[1]
Publication Abstract from PubMed
Lipocalins are a superfamily of functionally diverse proteins defined by a well-conserved tertiary structure despite variation in sequence. Lipocalins bind and transport small hydrophobic molecules in organisms of all kingdoms. However, there is still uncertainty regarding the function of some members of the family, including bacterial lipocalin Blc from Escherichia coli. Here, we present evidence that lipocalin Blc may be involved in heme binding, trans-periplasmic transport, or heme storage. This conclusion is supported by a cocrystal structure, mass-spectrometric data, absorption titration, and in silico analysis. Binding of heme is observed at low micromolar range with one-to-one ligand-to-protein stoichiometry. However, the absence of classical coordination to the iron atom leaves the possibility that the primary ligand of Blc is another tetrapyrrole.
Lipocalin Blc is a potential heme-binding protein.,Bozhanova NG, Calcutt MW, Beavers WN, Brown BP, Skaar EP, Meiler J FEBS Lett. 2021 Jan;595(2):206-219. doi: 10.1002/1873-3468.14001. Epub 2020 Dec , 3. PMID:33210733[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Campanacci V, Nurizzo D, Spinelli S, Valencia C, Tegoni M, Cambillau C. The crystal structure of the Escherichia coli lipocalin Blc suggests a possible role in phospholipid binding. FEBS Lett. 2004 Mar 26;562(1-3):183-8. PMID:15044022 doi:10.1016/S0014-5793(04)00199-1
- ↑ Bozhanova NG, Calcutt MW, Beavers WN, Brown BP, Skaar EP, Meiler J. Lipocalin Blc is a potential heme-binding protein. FEBS Lett. 2021 Jan;595(2):206-219. PMID:33210733 doi:10.1002/1873-3468.14001
