1AT6

HEN EGG WHITE LYSOZYME WITH A ISOASPARTATE RESIDUE

1AT6 の概要

• エントリーDOI: 10.2210/pdb1at6/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: isoaspartate, hydrolase, o-glycosyl hydrolase
• 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

Noguchi, S.,Miyawaki, K.,Satow, Y. (登録日: 1997-08-19, 公開日: 1998-02-25, 最終更新日: 2024-11-20)

主引用文献

Noguchi, S.,Miyawaki, K.,Satow, Y.
Succinimide and isoaspartate residues in the crystal structures of hen egg-white lysozyme complexed with tri-N-acetylchitotriose.
J.Mol.Biol., 278:231-238, 1998

PubMed Abstract: The isomerization of Asp101 to isoaspartate autocatalytically proceeds via a succinimide intermediate in hen egg-white lysozyme at a mildly acidic condition. The crystal structures of succinimide and isoaspartate forms of the lysozyme proteins, each complexed with a tri-N-acetylchitotriose ligand, have been determined at 1.8 A resolution, and distinctively elucidate coplanar cyclic aminosuccinyl and beta-linked isoaspartyl residues. Compared with the liganded native protein with normal Asp101, succinimide 101 protrudes toward the ligand, and isoaspartate 101 extends away from the ligand. The formations of these residues caused the loss of three hydrogen-bonds between the ligand and the side-chains of Asp101 and Asn103 along with 0.5 A displacement of the ligand location.

PubMed: 9571046
DOI: 10.1006/jmbi.1998.1674

実験手法

X-RAY DIFFRACTION (1.8 Å)