1AYY

GLYCOSYLASPARAGINASE

1AYY の概要

• エントリーDOI: 10.2210/pdb1ayy/pdb
• 分子名称: GLYCOSYLASPARAGINASE (3 entities in total)
• 機能のキーワード: glycoamidase, hydrolase
• 由来する生物種: Elizabethkingia meningoseptica; 詳細
• 細胞内の位置: Periplasm: Q47898 Q47898
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 64395.30

構造登録者

Van Roey, P.,Xuan, J. (登録日: 1997-11-12, 公開日: 1998-04-29, 最終更新日: 2024-04-03)

主引用文献

Xuan, J.,Tarentino, A.L.,Grimwood, B.G.,Plummer Jr., T.H.,Cui, T.,Guan, C.,Van Roey, P.
Crystal structure of glycosylasparaginase from Flavobacterium meningosepticum.
Protein Sci., 7:774-781, 1998

PubMed Abstract: The crystal structure of recombinant glycosylasparaginase from Flavobacterium meningosepticum has been determined at 2.32 angstroms resolution. This enzyme is a glycoamidase that cleaves the link between the asparagine and the N-acetylglucosamine of N-linked oligosaccharides and plays a major role in the degradation of glycoproteins. The three-dimensional structure of the bacterial enzyme is very similar to that of the human enzyme, although it lacks the four disulfide bridges found in the human enzyme. The main difference is the absence of a small random coil domain at the end of the alpha-chain that forms part of the substrate binding cleft and that has a role in the stabilization of the tetramer of the human enzyme. The bacterial glycosylasparaginase is observed as an (alphabeta)2-tetramer in the crystal, despite being a dimer in solution. The study of the structure of the bacterial enzyme allows further evaluation of the effects of disease-causing mutations in the human enzyme and confirms the suitability of the bacterial enzyme as a model for functional analysis.

PubMed: 9541410

実験手法

X-RAY DIFFRACTION (2.32 Å)