1IP2

G48A HUMAN LYSOZYME

1IP2 の概要

• エントリーDOI: 10.2210/pdb1ip2/pdb
• 関連するPDBエントリー: 1GDW 1IP1 1IP3 1IP4 1IP5 1IP6 1IP7
• 分子名称: LYSOZYME C, SODIUM ION (3 entities in total)
• 機能のキーワード: 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: 14757.71

構造登録者

Takano, K.,Yamagata, Y.,Yutani, K. (登録日: 2001-04-20, 公開日: 2001-11-14, 最終更新日: 2023-12-27)

主引用文献

Takano, K.,Yamagata, Y.,Yutani, K.
Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein.
Proteins, 45:274-280, 2001

PubMed Abstract: Our previous study of six non-Gly to Gly/Ala mutant human lysozymes in a left-handed helical region showed that only one non-Gly residue at a rigid site had unfavorable strain energy as compared with Gly at the same position (Takano et al., Proteins 2001; 44:233-243). To further examine the role of left-handed residues in the conformational stability of a protein, we constructed ten Gly to Ala mutant human lysozymes. Most Gly residues in human lysozyme are located in the left-handed helix region. The thermodynamic parameters for denaturation and crystal structures were determined by differential scanning calorimetry and X-ray analysis, respectively. The difference in denaturation Gibbs energy (DeltaDeltaG) for the ten Gly to Ala mutants ranged from + 1.9 to -7.5 kJ/mol, indicating that the effect of the mutation depends on the environment of the residue. We confirm that Gly in a left-handed region is more favorable at rigid sites than non-Gly, but there is little difference in energetic cost between Gly and non-Gly at flexible sites. The present results indicate that dihedral angles in the backbone conformation and also the flexibility at the position should be considered for analyses of protein stability, and protein structural determination, prediction, and design.

PubMed: 11599030
DOI: 10.1002/prot.1147

実験手法

X-RAY DIFFRACTION (1.8 Å)