3AJN

Structural basis of glycine amide on suppression of protein aggregation by high resolution X-ray analysis

「2ZXS」から置き換えられました

3AJN の概要

• エントリーDOI: 10.2210/pdb3ajn/pdb
• 分子名称: Lysozyme C, AMINOMETHYLAMIDE, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, lysozyme, glycosidase, glycine amide
• 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: 14721.38

構造登録者

Ito, L.,Shiraki, K.,Hasegawa, K.,Kumasaka, T. (登録日: 2010-06-09, 公開日: 2011-02-16, 最終更新日: 2024-10-23)

主引用文献

Ito, L.,Shiraki, K.,Makino, M.,Hasegawa, K.,Kumasaka, T.
Glycine amide shielding on the aromatic surfaces of lysozyme: Implication for suppression of protein aggregation
Febs Lett., 585:555-560, 2011

PubMed Abstract: Glycine amide (GlyAd), a typically amidated amino acid, is a versatile additive that suppresses protein aggregation during refolding, heat treatment, and crystallization. In spite of its effectiveness, the exact mechanism by which GlyAd suppresses protein aggregation remains to be elucidated. Here, we show the crystal structure of the GlyAd-lysozyme complex by high resolution X-ray crystallographic analysis at a 1.05Å resolution. GlyAd bound to the lysozyme surface near aromatic residues and decreased the amount of bound waters and increased the mobility of protein. Arg and GlyAd molecules are different in binding sites and patterns from glycerol and related compounds, indicating that decreasing hydrophobic patches might be involved in suppression of protein aggregation.

PubMed: 21237160
DOI: 10.1016/j.febslet.2011.01.008

実験手法

X-RAY DIFFRACTION (1.05 Å)