Crystal Structures of Human and Bacterial arylsulfatases
Malfunction of sulfatases leads in humans to severe
genetic diseases. The structure of ASA was determined at 2.1 Å resolution
in a colaboration between the group of Prof. K. von Figura, Dr. Schmidt
and PD. Dr. Dierks (Biochemie II, Göttingen) and the group of Prof.
W. Saenger (Kristallographie, Freie Universität Berlin). ASB
was determined at 2.5 Å in the laboratory of Prof. J.M. Guss (University
Due to the limited resolution in these structures, two contradictory catalytic
mechanisms were derived. In order to establish unequivocally the catalytic
mechanism for sulfate ester hydrolysis, the structures of ASA mutants alone
and in complex with the synthetic substrate p-nitrocatecholsulfate
were determined at resolutions around 2.5 Å in a collaboration between
our group and the Department Biochemie II at the Medizin Fakultät, Göttingen.
These structures gave insight into the coordination of the substrate during
catalysis in the absence of the covalent bond to the key catalytic residue,
and on the behaviour of partially inactive mutants. Still, the resolution
of these structures remained a limitation. The nature of the active site
could be established in the structure of a sulfatase.