PebB from the cryptophyte Guillardia theta binds the natural substrate biliverdin in a flipped orientation in comparison to the canonical binding orientation observed in this enzyme family. The resulting insights into protein function were deemed of sufficient interest to warrant publication in JBC!
In this study with colleagues from Jülich, we were able to reprogram an enzyme to work as a histidin biosensor. Published in Nat. Comm.
The groups Hemschemeier and Hofmann were able to resolve the 3D structure of truncated hemoglobin THB11 from Chlamydomonas reinhardtii.
Prof. Dr. Eckhard Hofmann
Welcome to the group 'Röntgenstrukturanalyse an Proteinen'!
We investigate structure and function of proteins. We use X-ray protein crystallography to unravel the 3D structures of proteins to get the insights into the arrangements of active sites. The combination with biophysical and biochemical methods is essential to investigate the mechanistical details of catalysis or transport. One focus of our projects involves integral or associated membrane proteins.