1hdh
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ARYLSULFATASE FROM PSEUDOMONAS AERUGINOSA
OverviewOverview
BACKGROUND: Sulfatases constitute a family of enzymes with a highly, conserved active site region including a Calpha-formylglycine that is, posttranslationally generated by the oxidation of a conserved cysteine or, serine residue. The crystal structures of two human arylsulfatases, ASA, and ASB, along with ASA mutants and their complexes led to different, proposals for the catalytic mechanism in the hydrolysis of sulfate esters., RESULTS: The crystal structure of a bacterial sulfatase from Pseudomonas, aeruginosa (PAS) has been determined at 1.3 A. Fold and active site region, are strikingly similar to those of the known human sulfatases. The, structure allows a precise determination of the active site region, unequivocally showing the presence of a Calpha-formylglycine hydrate as, the ... [(full description)]
About this StructureAbout this Structure
1HDH is a [Single protein] structure of sequence from [Pseudomonas aeruginosa] with CA and SO4 as [ligands]. Active as [Arylsulfatase], with EC number [3.1.6.1]. Structure known Active Site: CA1. Full crystallographic information is available from [OCA].
ReferenceReference
1.3 A structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family., Boltes I, Czapinska H, Kahnert A, von Bulow R, Dierks T, Schmidt B, von Figura K, Kertesz MA, Uson I, Structure. 2001 Jun;9(6):483-91. PMID:11435113
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