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Lipocalin Blc is a potential heme-binding protein

Journal Article · · FEBS Letters
 [1];  [2];  [2];  [1];  [2];  [3]
  1. Vanderbilt Univ., Nashville, TN (United States)
  2. Vanderbilt Univ. School of Medicine, Nashville, TN (United States)
  3. Vanderbilt Univ., Nashville, TN (United States); Leipzig Univ. (Germany)
+ Show Author Affiliations
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.
Research Organization:
Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Organization:
National Institutes of Health (NIH); USDOE Office of Science (SC)
Grant/Contract Number:
AC02-06CH11357
OSTI ID:
1765208
Alternate ID(s):
OSTI ID: 1766180
Journal Information:
FEBS Letters, Journal Name: FEBS Letters Journal Issue: 2 Vol. 595; ISSN 0014-5793
Publisher:
Federation of European Biochemical SocietiesCopyright Statement
Country of Publication:
United States
Language:
ENGLISH

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Related Subjects

59 BASIC BIOLOGICAL SCIENCES
Blc
crystal structure
hematoporphyrin
heme-binding protein
lipocalins