6DEY

Aspartylglucosaminuria mutant structure and function

6DEY の概要

• エントリーDOI: 10.2210/pdb6dey/pdb
• 分子名称: Glycosylasparaginase, residues 38-178, Glycosylasparaginase, residues 188-331 (3 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Elizabethkingia meningoseptica (Chryseobacterium meningosepticum); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 62150.96

構造登録者

Pande, S.,Laksminarasimhan, D.,Guo, H.C. (登録日: 2018-05-13, 公開日: 2018-08-01, 最終更新日: 2024-03-13)

主引用文献

Pande, S.,Bizilj, W.,Guo, H.C.
Biochemical and structural insights into an allelic variant causing the lysosomal storage disorder - aspartylglucosaminuria.
FEBS Lett., 592:2550-2561, 2018

PubMed Abstract: Aspartylglucosaminuria (AGU) is a lysosomal storage disorder caused by defects of the hydrolase glycosylasparaginase (GA). Previously, we showed that a Canadian AGU mutation disrupts an obligatory intramolecular autoprocessing with the enzyme trapped as an inactive precursor. Here, we report biochemical and structural characterizations of a model enzyme corresponding to a Finnish AGU allele, the T234I variant. Unlike the Canadian counterpart, the Finnish variant is capable of a slow autoprocessing to generate detectible hydrolyzation activity of the natural substrate of GA. We have determined a 1.6 Å-resolution structure of the Finnish AGU model and built an enzyme-substrate complex to provide a structural basis for analyzing the negative effects of the point mutation on K and k of the mature enzyme.

PubMed: 29993127
DOI: 10.1002/1873-3468.13190

実験手法

X-RAY DIFFRACTION (1.63 Å)