1Y1E: Human Formylglycine Generating Enzyme

Citation:
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.
PDB ID: 1Y1EDownload
MMDB ID: 33160
PDB Deposition Date: 2004/11/18
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 1.73  Å
Source Organism:
Similar Structures:
Biological Unit for 1Y1E: monomeric; determined by author
Molecular Components in 1Y1E
Label Count Molecule
Protein (1 molecule)
1
C-alpha-formyglycine-generating Enzyme(Gene symbol: SUMF1)
Molecule annotation
Chemicals (3 molecules)
1
1
2
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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