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. Cl coordination site. 1st Ca coordination site. 2nd Ca coordination site.

3D structures of sulfatase-modifying factor

Updated on 13-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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