1FSU

Crystal Structure of 4-Sulfatase (human)

1FSU の概要

• エントリーDOI: 10.2210/pdb1fsu/pdb
• 分子名称: N-ACETYLGALACTOSAMINE-4-SULFATASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: sulfatase, glycosaminoglycan degradation, hydrolase, glycoprotein, lysosome
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Lysosome: P15848
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56743.41

構造登録者

Bond, C.,Guss, M. (登録日: 1996-07-29, 公開日: 1998-02-04, 最終更新日: 2025-03-26)

主引用文献

Bond, C.S.,Clements, P.R.,Ashby, S.J.,Collyer, C.A.,Harrop, S.J.,Hopwood, J.J.,Guss, J.M.
Structure of a human lysosomal sulfatase.
Structure, 5:277-289, 1997

PubMed Abstract: . Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates including glycosaminoglycans, glycolipids and steroids. There is sufficient common sequence similarity within the class of sulfatase enzymes to indicate that they have a common structure. Deficiencies of specific lysosomal sulfatases that are involved in the degradation of glycosamino-glycans lead to rare inherited clinical disorders termed mucopolysaccharidoses. In sufferers of multiple sulfatase deficiency, all sulfatases are inactive because an essential post-translational modification of a specific active-site cysteine residue to oxo-alanine does not occur. Studies of this disorder have contributed to location and characterization of the sulfatase active site. To understand the catalytic mechanism of sulfatases, and ultimately the determinants of their substrate specificities, we have determined the structure of N-acetylgalactosamine-4-sulfatase.

PubMed: 9032078
DOI: 10.1016/S0969-2126(97)00185-8

実験手法

X-RAY DIFFRACTION (2.5 Å)