2026-04-13T05:50:59Zhttps://recercat.cat/oai/request

oai:recercat.cat:2445/2229462025-12-19T20:48:52Zcom_2072_1057col_2072_478825col_2072_478917

00925njm 22002777a 4500 dc Sanz-Gaitero, Marta author De Maesschalck, Vincent author Patel, Ankur author Longin, Hannelore author Van Noort, Vera author Rodríguez-Rubio, Lorena author van Ryne, Michael author Danis-Wlodarczyk, Katarzyna author Drulis-Kawa, Zuzanna author Mesnage, Stephane author van Raaij, Mark author Lavigne, Rob author 2025-09-04T13:13:41Z 2025-09-04T13:13:41Z 2024-06-21 2025-09-04T13:13:41Z Background: Endolysins are phage-encoded lytic enzymes that degrade bacterial peptidoglycan at the end of phage lytic cycles to release new phage particles. These enzymes are being explored as an alternative to small-molecule antibiotics. Methods: The crystal structure of KTN6 Gp46 was determined and compared with a ColabFold model. Cleavage specificity was examined using a peptidoglycan digest and reversed-phase high-performance liquid chromatography coupled to mass spectrometry (HPLC/MS). Results: The structure of KTN6 Gp46 could be determined at 1.4 Å resolution, and key differences in loops of the putative peptidoglycan binding domain were identified in comparison with its closest known homologue, the endolysin of phage SPN1S. Reversed-phase HPLC/MS analysis of the reaction products following peptidoglycan digestion confirmed the muramidase activity of Gp46, consistent with structural predictions. Conclusion: These insights into the structure and function of endolysins further expand the toolbox for endolysin engineering and explore their potential in enzyme-based antibacterial design strategies. Lisina Hidrolases Bacteriòfags Lisozim Lysine Hydrolases Bacteriophages Lysozyme Structural and biochemical characterization of a new phage-encoded muramidase, KTN6 Gp46