Structural basis for the lysis trigger of endolysin targeting Clostridia bacteria
Abstract: Endolysins are bacteriophage proteins involved in the lysis of their bacterial hosts. They consist of a catalytic domain that digests the bacterial cell wall, and a cell wall binding domain that specifically binds to a small range of bacterial species. We have determined crystal structures of two endolysins that target pathogenic Clostridia species. The crystal structures provide clues how the endolysins are activated following a molecular trigger. Further experiments using SAXS, mutagenesis, mass spectroscopy and lysis assays reveal a mechanism that is probably widespread among anaerobic systems.
Rob Meijers is a scientist at EMBL Hamburg. His group investigates molecular recognition events involved in the reorganization of surface protein clusters during cell-cell interactions. His group is also responsible for running the Sample Preparation and Characterization facility in the new Petra III lab at DESY.