1TEW

STRUCTURE OF HEXAGONAL TURKEY EGG WHITE LYSOZYME AT 1.65 ANGSTROMS RESOLUTION

1TEW の概要

• エントリーDOI: 10.2210/pdb1tew/pdb
• 分子名称: TURKEY EGG WHITE LYSOZYME, THIOCYANATE ION (3 entities in total)
• 機能のキーワード: hydrolase(o-glycosyl)
• 由来する生物種: Meleagris gallopavo (turkey)
• 細胞内の位置: Secreted: P00703
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14286.19

構造登録者

Howell, P.L. (登録日: 1994-11-17, 公開日: 1995-01-26, 最終更新日: 2024-10-16)

主引用文献

Howell, P.L.
Structure of hexagonal turkey egg-white lysozyme at 1.65A resolution.
Acta Crystallogr.,Sect.D, 51:654-662, 1995

PubMed Abstract: The structure of hexagonal turkey egg-white lysozyme (TEWL) has been determined and refined at 1.65 A resolution. The crystals were grown from a 150 mM potassium thiocyanate solution at pH 4.5 and belong to space group P6(1)22 with unit-cell dimensions a = b = 70.96, c = 83.01 A alpha = beta = 90, gamma = 120 degrees. The crystals were isomorphous with those of hexagonal pH 8.0 TEWL. The coordinates of PDB entry code 3LZ2 were therefore used as the initial model and subjected to rigid-body refinement, simulated annealing and least-squares refinement to a final residual of 0.20. The root-mean-square deviations from the ideal bond distances and angles were 0.016 A and 2.2 degrees, respectively. During the refinement, 86 water molecules and one thiocyanate ion were located in the structure. The thiocyanate ion lies close to the interface between two symmetry-related molecules. The S atom of the ion forms two direct intermolecular contacts with Argl4 and interacts indirectly via a network of water molecules to Arg5 of a symmetry-related molecule. The structure provides direct evidence for the mode of thiocyanate binding to arginine residues and suggests a possible mechanism for the efficiency of thiocyanate in crystallizing basic proteins.

PubMed: 15299795
DOI: 10.1107/S0907444994013612

実験手法

X-RAY DIFFRACTION (1.65 Å)