1UIH

ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE AND CHARGED SIDE CHAINS

1UIH の概要

• エントリーDOI: 10.2210/pdb1uih/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900017
• 分子名称: LYSOZYME, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: hydrolase, glycosidase, electrostatic interaction, helix, hen lysozyme, stability
• 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: 14958.75

構造登録者

Motoshima, H.,Ohmura, T.,Ueda, T.,Imoto, T. (登録日: 1996-11-26, 公開日: 1997-11-26, 最終更新日: 2024-11-20)

主引用文献

Ohmura, T.,Motoshima, H.,Ueda, T.,Imoto, T.
Fluctuations in free or substrate-complexed lysozyme and a mutant of it detected on x-ray crystallography and comparison with those detected on NMR.
J.Biochem.(Tokyo), 131:701-704, 2002

PubMed Abstract: A mutant lysozyme in which Arg14 and His15 were deleted together exhibited higher activity toward glycol chitin than the wild-type lysozyme. Moreover, the mutant lysozyme, which is less stable than the wild-type lysozyme by 7 degrees C, showed a shift of temperature dependence of activity to the low temperature side compared with the wild-type lysozyme [Protein Eng. 7, 743-748 (1994)]. In the free enzyme, the internal motion of the mutant lysozyme was similar to that of the wild-type. The internal motions of the wild-type and mutant lysozymes in the enzyme-substrate complex increased more than those in the free enzymes. Moreover, the increased internal motions of the substrate-complexed mutant lysozyme were greater than those of the substrate-complexed wild-type lysozyme in several residues [J. Mol. Biol. 286, 1547-1565 (1999)]. The structure of the mutant lysozyme was very similar to that of the wild-type lysozyme. Both structures were also alike in the complex of the trimer of N-acetyl-D-glucosamine. The mobility from B-factors agreed to some degree with that from order parameters in the regions showing great mobility of the protein, but this was not the case in the regions showing fast motion. However, we came to the same conclusion that the increased activity of the mutant lysozyme is due to the increase in the fluctuation of the lysozyme molecule. B-factor and order parameter do not always exhibit harmony because the time-scale of the analysis of mobility is different. However, they are not incompatible but complementary for detecting precise protein motions.

PubMed: 11983077

実験手法

X-RAY DIFFRACTION (1.75 Å)