1FSU

Crystal Structure of 4-Sulfatase (human)

Summary for 1FSU

• Entry DOI: 10.2210/pdb1fsu/pdb
• Descriptor: N-ACETYLGALACTOSAMINE-4-SULFATASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: sulfatase, glycosaminoglycan degradation, hydrolase, glycoprotein, lysosome
• Biological source: Homo sapiens (human)
• Cellular location: Lysosome: P15848
• Total number of polymer chains: 1
• Total formula weight: 56743.41

Authors

Bond, C.,Guss, M. (deposition date: 1996-07-29, release date: 1998-02-04, Last modification date: 2025-03-26)

Primary citation

Bond, C.S.,Clements, P.R.,Ashby, S.J.,Collyer, C.A.,Harrop, S.J.,Hopwood, J.J.,Guss, J.M.
Structure of a human lysosomal sulfatase.
Structure, 5:277-289, 1997

PubMed Abstract: . Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates including glycosaminoglycans, glycolipids and steroids. There is sufficient common sequence similarity within the class of sulfatase enzymes to indicate that they have a common structure. Deficiencies of specific lysosomal sulfatases that are involved in the degradation of glycosamino-glycans lead to rare inherited clinical disorders termed mucopolysaccharidoses. In sufferers of multiple sulfatase deficiency, all sulfatases are inactive because an essential post-translational modification of a specific active-site cysteine residue to oxo-alanine does not occur. Studies of this disorder have contributed to location and characterization of the sulfatase active site. To understand the catalytic mechanism of sulfatases, and ultimately the determinants of their substrate specificities, we have determined the structure of N-acetylgalactosamine-4-sulfatase.

PubMed: 9032078
DOI: 10.1016/S0969-2126(97)00185-8

Experimental method

X-RAY DIFFRACTION (2.5 Å)