1WQN

CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

1WQN の概要

• エントリーDOI: 10.2210/pdb1wqn/pdb
• 分子名称: LYSOZYME, SODIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase (o-glycosyl), glycosidase, bacteriolytic enzyme, 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: 14798.59

構造登録者

Yamagata, Y.,Kubota, M.,Sumikawa, Y.,Funahashi, J.,Fujii, S.,Yutani, K. (登録日: 1998-02-09, 公開日: 1998-07-01, 最終更新日: 2024-04-03)

主引用文献

Yamagata, Y.,Kubota, M.,Sumikawa, Y.,Funahashi, J.,Takano, K.,Fujii, S.,Yutani, K.
Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants.
Biochemistry, 37:9355-9362, 1998

PubMed Abstract: The contribution of hydrogen bonds to the conformational stability of human lysozyme was investigated by the combination of calorimetric and X-ray analyses of six Tyr --> Phe mutants. Unfolding Delta G and unfolding Delta H values of the Tyr --> Phe mutant proteins were changed by from +0.3 to -4.0 kJ/mol and from 0 to -16 kJ/mol, respectively, compared to those of the wild-type protein. The net contribution of a hydrogen bond at a specific site to stability (Delta Gwild/HB), considering factors affected by substitutions, was evaluated on the basis of X-ray structures of the mutant proteins. In the present study, one of six mutant proteins was suitable for evaluating the strength of the hydrogen bond. Delta Gwild/HB for the intramolecular hydrogen bond at Tyr124 was evaluated to be 7.5 kJ/mol. Results of the analysis of other mutants also suggest that hydrogen bonds of the hydroxyl group of Tyr, including the hydrogen bond with a water molecule, contribute to the stabilization of the human lysozyme.

PubMed: 9649316
DOI: 10.1021/bi980431i

実験手法

X-RAY DIFFRACTION (1.8 Å)