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1GFJ

CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

1GFJ の概要
エントリーDOI10.2210/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: 2023-12-27)
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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.8 Å)
構造検証レポート
Validation report summary of 1gfj
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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