1auk
From Proteopedia
|
HUMAN ARYLSULFATASE A
Overview
Human lysosomal arylsulfatase A (ASA) is a prototype member of the, sulfatase family. These enzymes require the posttranslational oxidation of, the -CH2SH group of a conserved cysteine to an aldehyde, yielding a, formylglycine. Without this modification sulfatases are catalytically, inactive, as revealed by a lysosomal storage disorder known as multiple, sulfatase deficiency. The 2.1 A resolution X-ray crystal structure shows, an ASA homooctamer composed of a tetramer of dimers, (alpha 2)4. The, alpha/beta fold of the monomer has significant structural analogy to, another hydrolytic enzyme, the alkaline phosphatase, and superposition of, these two structures shows that the active centers are located in largely, identical positions. The functionally essential formylglycine is located, in a ... [(full description)]
About this Structure
1AUK is a [Single protein] structure of sequence from [Homo sapiens] with MG as [ligand]. Active as [[1]], with EC number [3.1.6.8]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis., Lukatela G, Krauss N, Theis K, Selmer T, Gieselmann V, von Figura K, Saenger W, Biochemistry. 1998 Mar 17;37(11):3654-64. PMID:9521684
Page seeded by OCA on Mon Oct 29 21:05:31 2007
