1LAA

X-RAY STRUCTURE OF GLU 53 HUMAN LYSOZYME

1LAA の概要

• エントリーDOI: 10.2210/pdb1laa/pdb
• 分子名称: HUMAN LYSOZYME (2 entities in total)
• 機能のキーワード: hydrolase (o-glycosyl)
• 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: 14734.72

構造登録者

Harata, K.,Muraki, M.,Jigami, Y. (登録日: 1992-06-24, 公開日: 1993-01-15, 最終更新日: 2024-11-20)

主引用文献

Harata, K.,Muraki, M.,Hayashi, Y.,Jigami, Y.
X-ray structure of Glu 53 human lysozyme.
Protein Sci., 1:1447-1453, 1992

PubMed Abstract: The three-dimensional structure of a modified human lysozyme (HL), Glu 53 HL, in which Asp 53 was replaced by Glu, has been determined at 1.77 A resolution by X-ray analysis. The backbone structure of Glu 53 HL is essentially the same as the structure of wild-type HL. The root mean square difference for the superposition of equivalent C alpha atoms is 0.141 A. Except for the Glu 53 residue, the structure of the active site region is largely conserved between Glu 53 HL and wild-type HL. However, the hydrogen bond network differs because of the small shift or rotation of side chain groups. The carboxyl group of Glu 53 points to the carboxyl group of Glu 35 with a distance of 4.7 A between the nearest carboxyl oxygen atoms. A water molecule links these carboxyl groups by a hydrogen bond bridge. The active site structure explains well the fact that the binding ability for substrates does not significantly differ between Glu 53 HL and wild-type HL. On the other hand, the positional and orientational change of the carboxyl group of the residue 53 caused by the mutation is considered to be responsible for the low catalytic activity (ca. 1%) of Glu 53 HL. The requirement of precise positioning for the carboxyl group suggests the possibility that the Glu 53 residue contributes more than a simple electrostatic stabilization of the intermediate in the catalysis reaction.

PubMed: 1363898

実験手法

X-RAY DIFFRACTION (1.77 Å)