Lytic polysaccharide monooxygenases (LPMOs) are enzymes with a characteristic copper site (His brace) being able to degrade recalcitrant polysaccharides and with additional implications in microbial pathogenesis of humans and important crop plants.
This pilot project is a collaboration between the University of Copenhagen (UCPH) and the MAX IV facility in Sweden. It builds on UCPH’s extensive knowledge and crystallographic studies of the model LPMO and MAX IV’s cutting-edge serial crystallography capabilities. The results could enhance our understanding of LPMOs, leading to industrial applications in biofuels and new strategies for combating pathogens. Additionally, the collaboration will contribute to optimizing time-resolved crystallography techniques at MAX IV, benefiting future research endeavors.
Single crystal structure studies of microbial LPMOs at cryo-temperatures have been instrumental in elucidating their structure-function relationship, and have been the basis for mutagenesis, protein engineering and computational chemistry aimed at understanding the details of the reaction.
Serial crystallography emerges as a promising technique to capture the dynamic process of LPMOs’ action in a time-resolved manner, as it can be carried out at room temperature, potentially providing a deeper understanding of their catalytic mechanism at the molecular level. This knowledge could lead to optimized industrial applications and innovative strategies in pathogen control. In order to use serial crystallography for a time-resolved study, the reaction must be triggered in a controlled manner, and the triggering mechanism is a specific focus of this pilot project.
For further information please contact:
Leila Lo Leggio
University of Copenhagen
leila@chem.ku.dk