1LKR

MONOCLINIC HEN EGG WHITE LYSOZYME IODIDE

1LKR の概要

• エントリーDOI: 10.2210/pdb1lkr/pdb
• 分子名称: LYSOZYME, IODIDE ION (3 entities in total)
• 機能のキーワード: hydrolase, glycosidase, lysozyme
• 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: 2
• 化学式量合計: 30819.69

構造登録者

Steinrauf, L.K. (登録日: 1998-01-20, 公開日: 1998-04-29, 最終更新日: 2024-06-05)

主引用文献

Steinrauf, L.K.
Structures of monoclinic lysozyme iodide at 1.6 A and of triclinic lysozyme nitrate at 1.1 A.
Acta Crystallogr.,Sect.D, 54:767-780, 1998

PubMed Abstract: Hen egg-white lysozyme is one of the most thoroughly studied of enzymes and has been the subject of study by many methods, including X-ray crystallography. The present work extends the X-ray crystallography to higher resolution, includes the positions of the anions, and examines the contacts of the neighbors in greater detail. Data were collected at room temperature on a Rigaku R-axis area detector with rotating-anode X-ray generator to 1.6 A resolution for monoclinic lysozyme iodide at pH 4.0, to 1.8 A for monoclinic lysozyme iodide at pH 8.0, and to 1.1 A resolution for triclinic lysozyme nitrate at pH 4.5. The structures have been refined by SHELX93 with the expected number of anion sites being accounted for. Two regions of the protein have been found to be variable: residues 65-75 and 99-104. Except for 65-75 and 99-104, lysozyme is a very stable molecule with the crystal forms being held together by the electrostatic contacts of the anions and by layers of water molecules. The anion positions can be described as paired half sites, each half being contributed by a different lysozyme molecule. The many different crystal forms of lysozyme may be due to different combinations of the many such half sites on the surface. A hypothesis is presented for lysozyme in the different crystal forms and which may be extended to behavior in solution. Suggestions for future crystallographic research are proposed, involving anions of different shape and charge.

PubMed: 9757091
DOI: 10.1107/S0907444997016922

実験手法

X-RAY DIFFRACTION (1.6 Å)