3AGI

High resolution X-ray analysis of Arg-lysozyme complex in the presence of 500 mM Arg

3AGI の概要

• エントリーDOI: 10.2210/pdb3agi/pdb
• 関連するPDBエントリー: 3A34 3AGG 3AGH
• 分子名称: Lysozyme C, ACETATE ION, ARGININE, ... (6 entities in total)
• 機能のキーワード: hydrolase, lysozyme, glycosidase, arginine, allergen, antimicrobial, bacteriolytic enzyme, disulfide bond
• 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: 15222.44

構造登録者

Ito, L.,Shiraki, K.,Hasegawa, K.,Baba, S.,Kumasaka, T. (登録日: 2010-03-31, 公開日: 2011-03-23, 最終更新日: 2024-10-30)

主引用文献

Ito, L.,Shiraki, K.,Matsuura, T.,Okumura, M.,Hasegawa, K.,Baba, S.,Yamaguchi, H.,Kumasaka, T.
High-resolution X-ray analysis reveals binding of arginine to aromatic residues of lysozyme surface: implication of suppression of protein aggregation by arginine
Protein Eng.Des.Sel., 24:269-274, 2011

PubMed Abstract: While biotechnological applications of arginine (Arg) as a solution additive that prevents protein aggregation are increasing, the molecular mechanism of its effects remains unclear. In this study, we investigated the Arg-lysozyme complex by high-resolution crystallographic analysis. Three Arg molecules were observed to be in close proximity to aromatic amino acid residues of the protein surface, and their occupancies gradually increased with increasing Arg concentration. These interactions were mediated by electrostatic, hydrophobic and cation-π interactions with the surface residues. The binding of Arg decreased the accessible surface area of aromatic residues by 40%, but increased that of charged residues by 10%. These changes might prevent intermolecular hydrophobic interactions by shielding hydrophobic regions of the lysozyme surface, resulting in an increase in protein solubility.

PubMed: 21084280
DOI: 10.1093/protein/gzq101

実験手法

X-RAY DIFFRACTION (1.2 Å)