1Y1J

human formylglycine generating enzyme, sulfonic acid/desulfurated form

Summary for 1Y1J

• Entry DOI: 10.2210/pdb1y1j/pdb
• Related: 1Y1E 1Y1F 1Y1G 1Y1H 1Y1I
• Descriptor: C-alpha-formyglycine-generating enzyme, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: formylglycine, multiple sulfatase deficiency, cysteine sulfenic acid, oxidoreductase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 35682.52

Authors

Rudolph, M.G.,Dickmanns, A.,Ficner, R. (deposition date: 2004-11-18, release date: 2005-05-31, Last modification date: 2020-07-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.55 Å)