1LZN

NEUTRON STRUCTURE OF HEN EGG-WHITE LYSOZYME

1LZN の概要

• エントリーDOI: 10.2210/pdb1lzn/pdb
• 分子名称: PROTEIN (LYSOZYME), NITRATE ION, SODIUM ION, ... (4 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: 14664.17

構造登録者

Bon, C.I.,Lehmann, M.S.,Wilkinson, C. (登録日: 1999-03-23, 公開日: 1999-04-01, 最終更新日: 2024-11-13)

主引用文献

Bon, C.,Lehmann, M.S.,Wilkinson, C.
Quasi-Laue neutron-diffraction study of the water arrangement in crystals of triclinic hen egg-white lysozyme.
Acta Crystallogr.,Sect.D, 55:978-987, 1999

PubMed Abstract: Triclinic crystals of lysozyme, hydrogen-deuterium exchanged in deuterated solvent, have been studied using neutron quasi-Laue techniques and a newly developed cylinder image-plate detector. The wavelength range employed was from 2.7 to 3.5 A, which gave 9426 significant reflections [F >/= 2sigma(F)] to a resolution limit of 1. 7 A. The deuteration states of the H atoms in the protein molecule were identified, followed by an extensive analysis of the water structure surrounding the protein. The final R factor was 20.4% (Rfree = 22.1%). In total, the 244 observed water molecules form approximately one layer of water around the protein with far fewer water molecules located further away. Water molecules covering the apolar patches make tangential layers at 4-5 A from the surface or form C-H...O contacts, and several water-molecule sites can be identified in the apolar cavities. Many of the water molecules are apparently orientationally disordered, and only 115 out of the 244 water molecules sit in mean single orientations. Comparison of these results with quasi-elastic neutron scattering observations of the water dynamics leads to a picture of the water molecules forming an extended constantly fluctuating network covering the protein surface.

PubMed: 10216294
DOI: 10.1107/S0907444998018514

実験手法

NEUTRON DIFFRACTION (1.7 Å)