5F14

Structure of native hen egg-white lysozyme

5F14 の概要

• エントリーDOI: 10.2210/pdb5f14/pdb
• 関連するPDBエントリー: 1IEE 5F16
• 分子名称: Lysozyme C, SODIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: lysozyme, hydrolase
• 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: 14460.51

構造登録者

McGlone, C.,Nix, J.C.,Page, R.C. (登録日: 2015-11-30, 公開日: 2016-02-24, 最終更新日: 2024-10-23)

主引用文献

Lucius, M.,Falatach, R.,McGlone, C.,Makaroff, K.,Danielson, A.,Williams, C.,Nix, J.C.,Konkolewicz, D.,Page, R.C.,Berberich, J.A.
Investigating the Impact of Polymer Functional Groups on the Stability and Activity of Lysozyme-Polymer Conjugates.
Biomacromolecules, 17:1123-1134, 2016

PubMed Abstract: Polymers are often conjugated to proteins to improve stability; however, the impact of polymer chain length and functional groups on protein structure and function is not well understood. Here we use RAFT polymerization to grow polymers of different lengths and functionality from a short acrylamide oligomer with a RAFT end group conjugated to lysozyme. We show by X-ray crystallography that enzyme structure is minimally impacted by modification with the RAFT end group. Significant activity toward the negatively charged Micrococcus lysodeicticus cell wall was maintained when lysozyme was modified with cationic polymers. Thermal and chemical stability of the conjugates was characterized using differential scanning fluorimetry and tryptophan fluorescence. All conjugates had a lower melting temperature; however, conjugates containing ionic or substrate mimicking polymers were more resistant to denaturation by guanidine hydrochloride. Our results demonstrate that tailoring polymer functionality can improve conjugate activity and minimize enzymatic inactivation by denaturants.

PubMed: 26866284
DOI: 10.1021/acs.biomac.5b01743

実験手法

X-RAY DIFFRACTION (1.148 Å)