Sulfatase-modifying factor

spinqualitylabelsall models Glycosylated human sulfatase-modifying factor 1 (cyan) complex with arylsulfatase peptide (magenta), Ca+2 ion (green) and Cl- ion (green) (PDB code 2aij) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Sulfatase-modifying factor (SUMF) is an enzyme that catalyzes the hydrolysis of sulfate esters by oxidizing posttranslationally a cysteine residue in its substrate Sulfatase active site to 3-oxoalanine (C-α-formylglycine) residue. Disease Mutations in SUMF1 cause multiple sulfatase deficiency - a lysosomal storage disorder. SUMF1 is associated with chronic obstructive pulmonary disease. Structural highlights Glycosylated human sulfatase-modifying factor 1 complex with arylsulfatase peptide, Ca+2 ion and Cl- ion. The structure of SUMF1 complex with its substrate sulfatase terminal peptide CTPSR. SUMF1 active site contains 2 cysteine residues and mutating either of them to serine results in an inactive enzyme. Cys341 was found to be responsible for substrate binding and makes a Cys-Cys bond to the peptide cysteine residue. The peptide binds at the surface of SUMF1 in an extended conformation making numerous interactions with the protein.

3D structures of sulfatase-modifying factor

Updated on 10-December-2018

Sulfatase - hSUMF-1 - human
2aft, 2afy, 2hib, 2hi8 - hSUMF-1 (mutant)
2aij, 2aik - hSUMF-1 (mutant) + peptide
1y4j - hSUMF-2

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