1IR7
IM mutant of lysozyme
1IR7 の概要
| エントリーDOI | 10.2210/pdb1ir7/pdb |
| 関連するPDBエントリー | 1IR8 1IR9 |
| 分子名称 | lysozyme (2 entities in total) |
| 機能のキーワード | hydrolase, egg white |
| 由来する生物種 | Gallus gallus (chicken) |
| 細胞内の位置 | Secreted: P00698 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 14349.20 |
| 構造登録者 | |
| 主引用文献 | Ohmura, T.,Ueda, T.,Hashimoto, Y.,Imoto, T. Tolerance of point substitution of methionine for isoleucine in hen egg white lysozyme. Protein Eng., 14:421-425, 2001 Cited by PubMed Abstract: X-ray structure determination of proteins by using the multiple-wavelength anomalous dispersion method targeting selenomethionine is now widely employed. Isoleucine was examined for the second choice of the substitution of methionine next to leucine. We performed a systematic mutational study of the substitutions of methionine for isoleucine. All mutated lysozymes were less stable than the wild-type by about 1 kcal/mol and it is suggested that this instability was caused by the change in residual hydrophobicity from isoleucine to methionine. The X-ray structures of all mutant lysozymes were very similar to that of the wild-type. In addition, both the accessible surface areas and the conformation of the side chain of methionine in all mutant lysozymes were similar to those of the side chain at the respective isoleucine in the wild-type. Therefore, it is suggested that the mutation from isoleucine to methionine in a protein can be considered as a "safe" substitution. PubMed: 11477222DOI: 10.1093/protein/14.6.421 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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