1.3 Å Crystal Structure of a Bacterial Arylsulfatase.

The bacterial arylsulfatase from Pseudomonas aeruginosa (PAS) shows the same overall fold as the human arylsulfatases.
The active site is conserved among arylsulfatases. This allows a consensus mechanismus for sulfate ester cleavage to be derived for the arylsulfatase family.
 
 

foldactive site
 

The active site clearly reveals the presence of a formylglycine hydrate as the key catalytic sidechain. The metal is a calcium cation. A sulfate anion is found coordinated.


Sulfate ester cleavage mechanism in the sulfatase family.

This work was done in collaboration with the groups of Dr. Kertesz (Biological Sciences, Manchester) and Prof. von Figura, Dr. Schmidt and PD. Dr. Dierks (Biochemie II, Göttingen).
 
 
 

Some references.
 
 

Back to the first page. 









To the structures of immunoglobulin fragments (REI variants)  designed to be stabilized in the absence of the only disulphide bridge.