3LZ2

STRUCTURE DETERMINATION OF TURKEY EGG WHITE LYSOZYME USING LAUE DIFFRACTION

3LZ2 の概要

• エントリーDOI: 10.2210/pdb3lz2/pdb
• 分子名称: TURKEY EGG WHITE LYSOZYME (1 entity in total)
• 機能のキーワード: hydrolase(o-glycosyl)
• 由来する生物種: Meleagris gallopavo (turkey)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14228.10

構造登録者

Howell, P.L.,Almo, S.C.,Parsons, M.R.,Hajdu, J.,Petsko, G.A. (登録日: 1991-09-13, 公開日: 1993-10-31, 最終更新日: 2024-10-09)

主引用文献

Howell, P.L.,Almo, S.C.,Parsons, M.R.,Hajdu, J.,Petsko, G.A.
Structure determination of turkey egg-white lysozyme using Laue diffraction data.
Acta Crystallogr.,Sect.B, 48:200-207, 1992

PubMed Abstract: The three-dimensional structure of turkey egg-white lysozyme (TEWL) has been solved and refined at 2.5 A resolution using X-ray data collected by the Laue method. This is the first protein structure determination undertaken using Laue diffraction data. A re-examination of the existing structure of TEWL was necessary when attempts to refine an atomic model based on the C alpha positions in the Protein Data Bank (entry 1LZ2) failed. The correct orientation and position of the turkey lysozyme molecules within the crystallographic unit cell were determined by molecular replacement using a refined model of the homologous hen egg-white lysozyme crystal structure. After modification of the model to reflect the differences in amino-acid sequence between the chicken and turkey enzymes, the structure was subjected to crystallographic refinement using the simulated-annealing refinement technique and conventional least-squares refinement. This yielded a final residual of R = 20.7%. This crystal form is of potential interest for time-resolved crystallographic studies since the amino-acid residues involved in catalysis (Asp52 and Glu35) are accessible to solvent and not blocked by crystal contacts.

PubMed: 1515108
DOI: 10.1107/S0108768191012466

実験手法

X-RAY DIFFRACTION (2.5 Å)