5IO6

Bovine beta-lactoglobulin complex with dodecane, ambient pressure

5IO6 の概要

• エントリーDOI: 10.2210/pdb5io6/pdb
• 関連するPDBエントリー: 5IO5 5IO7
• 分子名称: Major allergen beta-lactoglobulin, DODECANE (3 entities in total)
• 機能のキーワード: beta-lactoglobulin, lipocalin, transport protein
• 由来する生物種: Bos taurus (Bovine)
• 細胞内の位置: Secreted : B5B0D4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18557.60

構造登録者

Kurpiewska, K.,Biela, A. (登録日: 2016-03-08, 公開日: 2016-03-16, 最終更新日: 2024-10-09)

主引用文献

Kurpiewska, K.,Biela, A.,Loch, J.I.,Swiatek, S.,Jachimska, B.,Lewinski, K.
Investigation of high pressure effect on the structure and adsorption of beta-lactoglobulin.
Colloids Surf B Biointerfaces, 161:387-393, 2017

PubMed Abstract: β-Lactoglobulin, being one of the principal whey protein, is of huge importance to the food industry. Temperature/pressure effects on this small protein has been extensively studied by industry. To characterize biochemical properties of β-lactoglobulin after or during pressurization, a wide range of methods have been used thus far. In this study, for the first time, the pressure-induced conformation of β-lactoglobulin in the crystal state was determined, at pressure 430 MPa. Changes observed in the high pressure structure correlate with the physico-chemical properties of pressure-treated β-lactoglobulin obtained from dynamic light scattering, electrophoretic mobility and quartz crystal microbalance with dissipation monitoring measurements. A comparison between the β-lactoglobulin structures determined at both high and ambient pressure contrasts the stable nature of the protein core and adjacent loop fragments. At high pressure the β-lactoglobulin structure presents early signs of dimer dissociation, charge and conformational changes characteristic for initial unfolded intermediate as well as a significant modification of the binding pocket volume. Those observations are supported by changes in zeta potential values and results in increase affinity of the β-lactoglobulin adsorption onto gold surface. Observed pressure-induced structural modifications were previously suggested as an important factor contributing to β-lactoglobulin denaturation process. Presented studies provide detailed analysis of pressure-associated structural changes influencing β-lactoglobulin conformation and consequently its adsorption.

PubMed: 29112912
DOI: 10.1016/j.colsurfb.2017.10.069

実験手法

X-RAY DIFFRACTION (2.851 Å)