1E06

Porcine Odorant Binding Protein Complexed with 5-methyl-2-(1-methylethyl)phenol

1E06 の概要

• エントリーDOI: 10.2210/pdb1e06/pdb
• 関連するPDBエントリー: 1A3Y 1DZJ 1DZK 1DZM 1DZP 1E00 1E02
• 分子名称: ODORANT-BINDING PROTEIN, 5-METHYL-2-(1-METHYLETHYL)PHENOL (3 entities in total)
• 機能のキーワード: odorant binding protein, lipocalins
• 由来する生物種: SUS SCROFA (PIG)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35743.26

構造登録者

Vincent, F.,Spinelli, S.,Cambillau, C.,Tegoni, M. (登録日: 2000-03-10, 公開日: 2000-12-06, 最終更新日: 2024-10-09)

主引用文献

Vincent, F.,Spinelli, S.,Ramoni, R.,Grolli, S.,Pelosi, P.,Cambillau, C.,Tegoni, M.
Complexes of Porcine Odorant Binding Protein with Odorant Molecules Belonging to Different Chemical Classes
J.Mol.Biol., 300:127-, 2000

PubMed Abstract: Porcine odorant binding protein (pOBP) is a monomer of 157 amino acid residues, purified in abundance from pig nasal mucosa. In contrast to the observation on lipocalins as retinol binding protein (RBP), major urinary protein (MUP) or bovine odorant binding protein (bOBP), no naturally occurring ligand was found in the beta-barrel cavity of pOBP. Porcine OBP was therefore chosen as a simple model for structure/function studies with odorant molecules. In competition experiments with tritiated pyrazine, the affinity of pOBP towards several odorant molecules belonging to different chemical classes has been found to be of the micromolar order, with a 1:1 stoichiometry. The X-ray structures of pOBP complexed to these molecules were determined at resolution between 2.15 and 1.4 A. As expected, the electron density of the odorant molecules was observed into the hydrophobic beta-barrel of the lipocalin. Inside this cavity, very few specific interactions were established between the odorant molecule and the amino acid side-chains, which did not undergo significant conformational change. The high B-factors observed for the odorant molecules as well as the existence of alternative conformations reveal a non-specific mode of binding of the odorant molecules in the cavity.

PubMed: 10864504
DOI: 10.1006/JMBI.2000.3820

実験手法

X-RAY DIFFRACTION (2.12 Å)