ASA ASB

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 of Sydney).
 

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.

  ASA-C69S ASA-C69A/pNCS
 
 

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 atomic resolution structure of a sulfatase.

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