1GFJ

CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

1GFJ の概要

• エントリーDOI: 10.2210/pdb1gfj/pdb
• 関連するPDBエントリー: 1GAY 1GF8 1GF9 1GFA 1GFE 1GFG 1GFH 1GFK 1GFR 1GFT 1GFU 1GFV 1INU
• 分子名称: LYSOZYME, SODIUM ION (3 entities in total)
• 機能のキーワード: surface, hydrophilic, stability, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P61626
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14759.64

構造登録者

Funahashi, J.,Takano, K.,Yamagata, Y.,Yutani, K. (登録日: 2000-12-04, 公開日: 2000-12-20, 最終更新日: 2024-11-20)

主引用文献

Funahashi, J.,Takano, K.,Yamagata, Y.,Yutani, K.
Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability.
J.Biol.Chem., 277:21792-21800, 2002

PubMed Abstract: Water molecules make a hydration structure with the network of hydrogen bonds, covering on the surface of proteins. To quantitatively estimate the contribution of the hydration structure to protein stability, a series of hydrophilic mutant human lysozymes (Val to Ser, Tyr, Asp, Asn, and Arg) modified at three different positions on the surface, which are located in the alpha-helix (Val-110), the beta-sheet (Val-2), and the loop (Val-74), were constructed. Their thermodynamic parameters of denaturation and crystal structures were examined by calorimetry and by x-ray crystallography at 100 K, respectively. The introduced polar residues made hydrogen bonds with protein atoms and/or water molecules, sometimes changing the hydration structure around the mutation site. Changes in the stability of the mutant proteins can be evaluated by a unique equation that considers the conformational changes resulting from the substitutions. Using this analysis, the relationship between the changes in the stabilities and the hydration structures for mutant human lysozymes substituted on the surface could be quantitatively estimated. The analysis indicated that the hydration structure on protein surface plays an important role in determining the conformational stability of the protein.

PubMed: 11927576
DOI: 10.1074/jbc.M110728200

実験手法

X-RAY DIFFRACTION (1.8 Å)