1P4K

CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT

1P4K の概要

• エントリーDOI: 10.2210/pdb1p4k/pdb
• 関連するPDBエントリー: 1P4V
• 分子名称: N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase, GLYCEROL (2 entities in total)
• 機能のキーワード: alpha beta, beta alpha, sandwich, hydrolase
• 由来する生物種: Elizabethkingia meningoseptica
• 細胞内の位置: Periplasm: Q47898
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64725.67

構造登録者

Qian, X.,Guan, C.,Guo, H.C. (登録日: 2003-04-23, 公開日: 2003-05-06, 最終更新日: 2024-02-14)

主引用文献

Qian, X.,Guan, C.,Guo, H.C.
A dual role for an aspartic acid in glycosylasparaginase autoproteolysis.
Structure, 11:997-1003, 2003

PubMed Abstract: Glycosylasparaginase uses an autoproteolytic processing mechanism, through an N-O acyl shift, to generate a mature/active enzyme from a single-chain precursor. Structures of glycosylasparaginase precursors in complex with a glycine inhibitor have revealed the backbone in the immediate vicinity of the scissile peptide bond to be in a distorted trans conformation, which is believed to be the driving force for the N-O acyl shift to break the peptide bond. Here we report the effects of point mutation D151N. In addition to the loss of the base essential in autoproteolysis, this mutation also eradicates the backbone distortion near the scissile peptide bond. Binding of the glycine inhibitor to the autoproteolytic site of the D151N mutant does not restore the backbone distortion. Therefore, Asp151 plays a dual role, acting as the general base to activate the nucleophile and holding the distorted trans conformation that is critical for initiating an N-O acyl shift.

PubMed: 12906830
DOI: 10.1016/S0969-2126(03)00150-3

実験手法

X-RAY DIFFRACTION (1.9 Å)