1Y1H

human formylglycine generating enzyme, oxidised Cys refined as hydroperoxide

1Y1H の概要

• エントリーDOI: 10.2210/pdb1y1h/pdb
• 関連するPDBエントリー: 1Y1E 1Y1F 1Y1G 1Y1I 1Y1J
• 分子名称: C-alpha-formyglycine-generating enzyme, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, STRONTIUM ION, ... (5 entities in total)
• 機能のキーワード: formylglycine, multiple sulfatase deficiency, cysteine sulfenic acid, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35542.30

構造登録者

Rudolph, M.G.,Dickmanns, A.,Ficner, R. (登録日: 2004-11-18, 公開日: 2005-05-31, 最終更新日: 2025-03-26)

主引用文献

Dierks, T.,Dickmanns, A.,Preusser-Kunze, A.,Schmidt, B.,Mariappan, M.,von Figura, K.,Ficner, R.,Rudolph, M.G.
Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme.
Cell(Cambridge,Mass.), 121:541-552, 2005

PubMed Abstract: Sulfatases are enzymes essential for degradation and remodeling of sulfate esters. Formylglycine (FGly), the key catalytic residue in the active site, is unique to sulfatases. In higher eukaryotes, FGly is generated from a cysteine precursor by the FGly-generating enzyme (FGE). Inactivity of FGE results in multiple sulfatase deficiency (MSD), a fatal autosomal recessive syndrome. Based on the crystal structure, we report that FGE is a single-domain monomer with a surprising paucity of secondary structure and adopts a unique fold. The effect of all 18 missense mutations found in MSD patients is explained by the FGE structure, providing a molecular basis of MSD. The catalytic mechanism of FGly generation was elucidated by six high-resolution structures of FGE in different redox environments. The structures allow formulation of a novel oxygenase mechanism whereby FGE utilizes molecular oxygen to generate FGly via a cysteine sulfenic acid intermediate.

PubMed: 15907468
DOI: 10.1016/j.cell.2005.03.001

実験手法

X-RAY DIFFRACTION (1.67 Å)