3E3C

Structure of GrlR-lipid complex

3E3C の概要

• エントリーDOI: 10.2210/pdb3e3c/pdb
• 関連するPDBエントリー: 2OVS
• 分子名称: L0044, (2R)-2-HYDROXY-3-(PHOSPHONOOXY)PROPYL HEXANOATE (3 entities in total)
• 機能のキーワード: grlr, lee regulator, lipid binding, lipid binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27010.70

構造登録者

Jobichen, C.,Sivaraman, J. (登録日: 2008-08-07, 公開日: 2009-04-07, 最終更新日: 2023-11-01)

主引用文献

Jobichen, C.,Fernandis, A.Z.,Velazquez-Campoy, A.,Leung, K.Y.,Mok, Y.K.,Wenk, M.R.,Sivaraman, J.
Identification and characterization of the lipid binding property of GrlR, a locus of enterocyte effacement regulator.
Biochem.J., 2009

PubMed 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.

PubMed: 19228114
DOI: 10.1042/BJ20081588

実験手法

X-RAY DIFFRACTION (2.5 Å)