 |
PDBsum entry 3e3c
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Lipid binding protein
|
PDB id
|
|
|
|
3e3c
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Identification and characterization of the lipid-Binding property of grlr, A locus of enterocyte effacement regulator.
|
|
|
Authors
|
|
C.Jobichen,
A.Z.Fernandis,
A.Velazquez-Campoy,
K.Y.Leung,
Y.K.Mok,
M.R.Wenk,
J.Sivaraman.
|
|
|
Ref.
|
|
Biochem J, 2009,
420,
191-199.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
