6F1M

Lysozyme crystallized in presence of 100 mM sodium phosphate at pH 4.5: low-humidity form

6F1M の概要

• エントリーDOI: 10.2210/pdb6f1m/pdb
• 分子名称: Lysozyme C (2 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Gallus gallus (Chicken)
• 細胞内の位置: Secreted: P00698
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14331.16

構造登録者

Camara-Artigas, A. (登録日: 2017-11-22, 公開日: 2018-05-09, 最終更新日: 2024-10-23)

主引用文献

Plaza-Garrido, M.,Salinas-Garcia, M.C.,Camara-Artigas, A.
Orthorhombic lysozyme crystallization at acidic pH values driven by phosphate binding.
Acta Crystallogr D Struct Biol, 74:480-489, 2018

PubMed Abstract: The structure of orthorhombic lysozyme has been obtained at 298 K and pH 4.5 using sodium chloride as the precipitant and in the presence of sodium phosphate at a concentration as low as 5 mM. Crystals belonging to space group P222 (unit-cell parameters a = 30, b = 56, c = 73 Å, α = β = γ = 90.00°) diffracted to a resolution higher than 1 Å, and the high quality of these crystals permitted the identification of a phosphate ion bound to Arg14 and His15. The binding of this ion produces long-range conformational changes affecting the loop containing Ser60-Asn74. The negatively charged phosphate ion shields the electrostatic repulsion of the positively charged arginine and histidine residues, resulting in higher stability of the phosphate-bound lysozyme. Additionally, a low-humidity orthorhombic variant was obtained at pH 4.5, and comparison with those previously obtained at pH 6.5 and 9.5 shows a 1.5 Å displacement of the fifth α-helix towards the active-site cavity, which might be relevant to protein function. Since lysozyme is broadly used as a model protein in studies related to protein crystallization and amyloid formation, these results indicate that the interaction of some anions must be considered when analysing experiments performed at acidic pH values.

PubMed: 29717719
DOI: 10.1107/S205979831800517X

実験手法

X-RAY DIFFRACTION (1.48 Å)