1CKC

T43A MUTANT HUMAN LYSOZYME

1CKC の概要

• エントリーDOI: 10.2210/pdb1ckc/pdb
• 分子名称: PROTEIN (LYSOZYME), SODIUM ION (3 entities in total)
• 機能のキーワード: stability, hydrogen bond, 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: 14713.66

構造登録者

Takano, K.,Yamagata, Y.,Funahashi, J.,Yutani, K. (登録日: 1999-04-22, 公開日: 1999-04-30, 最終更新日: 2024-11-13)

主引用文献

Takano, K.,Yamagata, Y.,Funahashi, J.,Hioki, Y.,Kuramitsu, S.,Yutani, K.
Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,).
Biochemistry, 38:12698-12708, 1999

PubMed Abstract: In globular proteins, there are intermolecular hydrogen bonds between protein and water molecules, and between water molecules, which are bound with the proteins, in addition to intramolecular hydrogen bonds. To estimate the contribution of these hydrogen bonds to the conformational stability of a protein, the thermodynamic parameters for denaturation and the crystal structures of five Thr to Val and five Thr to Ala mutant human lysozymes were determined. The denaturation Gibbs energy (DeltaG) of Thr to Val and Thr to Ala mutant proteins was changed from 4.0 to -5.6 kJ/mol and from 1.6 to -6.3 kJ/mol, respectively, compared with that of the wild-type protein. The contribution of hydrogen bonds to the stability (DeltaDeltaG(HB)) of the Thr and other mutant human lysozymes previously reported was extracted from the observed stability changes (DeltaDeltaG) with correction for changes in hydrophobicity and side chain conformational entropy between the wild-type and mutant structures. The estimation of the DeltaDeltaG(HB) values of all mutant proteins after removal of hydrogen bonds, including protein-water hydrogen bonds, indicates a favorable contribution of the intra- and intermolecular hydrogen bonds to the protein stability. The net contribution of an intramolecular hydrogen bond (DeltaG(HB[pp])), an intermolecular one between protein and ordered water molecules (DeltaG(HB[pw])), and an intermolecular one between ordered water molecules (DeltaG(HB[ww])) could be estimated to be 8. 5, 5.2, and 5.0 kJ/mol, respectively, for a 3 A long hydrogen bond. This result shows the different contributions to protein stability of intra- and intermolecular hydrogen bonds. The entropic cost due to the introduction of a water molecule (DeltaG(H)()2(O)) could be also estimated to be about 8 kJ/mol.

PubMed: 10504240
DOI: 10.1021/bi9910169

実験手法

X-RAY DIFFRACTION (1.8 Å)