1LYD

CRYSTAL STRUCTURE OF T4-LYSOZYME GENERATED FROM SYNTHETIC CODING DNA EXPRESSED IN ESCHERICHIA COLI

1LYD の概要

• エントリーDOI: 10.2210/pdb1lyd/pdb
• 分子名称: T4 LYSOZYME (2 entities in total)
• 機能のキーワード: hydrolase (o-glycosyl)
• 由来する生物種: Enterobacteria phage T4
• 細胞内の位置: Host cytoplasm : P00720
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18662.47

構造登録者

Rose, D.R. (登録日: 1989-01-11, 公開日: 1990-04-15, 最終更新日: 2024-02-14)

主引用文献

Rose, D.R.,Phipps, J.,Michniewicz, J.,Birnbaum, G.I.,Ahmed, F.R.,Muir, A.,Anderson, W.F.,Narang, S.
Crystal structure of T4-lysozyme generated from synthetic coding DNA expressed in Escherichia coli.
Protein Eng., 2:277-282, 1988

PubMed Abstract: The polypeptide produced by expressing a chemically synthesized gene coding for the amino-acid sequence of T4-lysozyme has been crystallized and subjected to X-ray diffraction. The crystal structure has been refined to a standard R-factor of 0.191 for data between 8 and 2 A resolution. The refined model is essentially the same as the well-known structure of wild-type T4-lysozyme determined previously by Matthews et al. (1987). Some small changes in the C-terminal region, which is important in maintaining the folded structure, have been noted. In addition to confirming that the synthetic gene product is very close to the wild type, this structure provides a benchmark for protein engineering experiments on the folding and the catalytic activity of this molecule by the method of gene synthesis.

PubMed: 3074306
DOI: 10.1093/protein/2.4.277

実験手法

X-RAY DIFFRACTION (2 Å)