Structure/Function-studies of enzymes

Description of Research Group

A common focus of many of the previous research projects has been on structural and/or biochemical characterization of proteins involved in environmental adaptation, either to low temperature and increased salinity, or to radiation-resistance.

Proteins and protein classes previously studied are: proteases (trypsin, subtilisin), antibiotic resistance proteins (MBLs, TmrD), DNA cleansing, modification and repair (SOD, UNG, MUG, EndA, hSMUG1, AlkA, RecO, RecR, DpnI, ParI), sugar binding and metabolism (α-mannosidase, maltooligosyltrehalose trehalohydrolase, Cel6a, Tr5), phospholipase D, protein kinase A, isocitrate dehydrogenase, L-lactate oxidase, GTPase, phenylalanine hydroxylase, as well as iron metabolism (SOD, ferric uptake regulator).
Present and future research will focus on the ectoine biosynthesis pathway, where we aim to functionally and structurally investigate the 4 enzymes (EctABCD) involved in biosynthesis of the osmoprotectants ectoine and hydroxyectoineas. These compounds have a pronounced effect in stabilizing both organisms and single proteins under stress conditions, and as such justifies further study. Furthermore, in some organisms, an ectoine degradation pathway exists containing the proteins doeABCD, which will be future highly relevant protein targets to investigate.

Methods used include:

• Standard molecular biology and biochemical characterization pipeline leading to crystal structures.

Technology, expertise and equipment

Technology and equipment as for other NorStruct members with respect to protein crystallization, data collection, structure determination and analysis.

Additional technology and expertise includes particular insight into challenging crystallographic problems in determining new crystal structures.