1BGI

ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH TEMPERATURE (310K)

1BGI の概要

• エントリーDOI: 10.2210/pdb1bgi/pdb
• 分子名称: LYSOZYME, CHLORIDE ION (3 entities in total)
• 機能のキーワード: hydrolase, o-glycosyl
• 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: 14366.61

構造登録者

Oki, H.,Matsuura, Y.,Komatsu, H.,Chernov, A.A. (登録日: 1998-05-28, 公開日: 1998-10-28, 最終更新日: 2024-10-30)

主引用文献

Oki, H.,Matsuura, Y.,Komatsu, H.,Chernov, A.A.
Refined structure of orthorhombic lysozyme crystallized at high temperature: correlation between morphology and intermolecular contacts.
Acta Crystallogr.,Sect.D, 55:114-121, 1999

PubMed Abstract: The structure of orthorhombic hen egg-white lysozyme (HEWL) crystallized at 310 K has been refined at 1.7 A resolution. Large displacements of the side-chain atoms with respect to the tetragonal structure were observed in many places, in contrast to small displacements of the main-chain atoms. A chloride-ion binding site was observed at an interface of two molecules, but at a different position to the binding site in the tetragonal form. The analysis of intermolecular contacts in the crystal has shown the presence of three independent intermolecular contacts which are called macrobonds A, B and C. Arginine side chains are frequently involved in these macrobonds, suggesting that the high frequency of this residue in HEWL may be a possible reason for the multiple polymorphs of this protein. The crystal forms were determined using a light-reflecting device on a four-circle diffractometer. Correlations between crystal forms and the three-dimensional macrobond networks were interpreted in terms of their components in various crystallographic planes, making use of approximate strengths of hydrogen-bond and van der Waals interatomic forces.

PubMed: 10089401
DOI: 10.1107/S0907444998008713

実験手法

X-RAY DIFFRACTION (1.7 Å)