9HTU
Structure of endolysin PlyP100 catalytic domain
Summary for 9HTU
Entry DOI | 10.2210/pdb9htu/pdb |
Descriptor | N-acetylmuramoyl-L-alanine amidase, ZINC ION, SULFATE ION, ... (4 entities in total) |
Functional Keywords | plyp100, endolysin, hydrolase |
Biological source | Listeria phage LP-125 |
Total number of polymer chains | 1 |
Total formula weight | 20117.84 |
Authors | Scaletti Hutchinson, E.,Stenmark, P. (deposition date: 2024-12-19, release date: 2025-06-25, Last modification date: 2025-07-02) |
Primary citation | Bateman, K.R.,Scaletti Hutchinson, E.,Widmalm, G.,Miller, M.J.,Stenmark, P. Structural and functional insights into Listeriamonocytogenes phage endolysin PlyP100: A promising food safety tool. J.Biol.Chem., 301:110295-110295, 2025 Cited by PubMed Abstract: Listeria monocytogenes is a ubiquitous, psychrotrophic human pathogen that can cause listeriosis, a serious illness for vulnerable populations. Some foods, such as Hispanic-style fresh cheeses like queso fresco, pose a specific risk because there are no widely accepted or available methods for L. monocytogenes mitigation that are both effective and able to maintain the properties of the products. Listeria-specific bacteriophages encode endolysins that are able to cleave the peptidoglycan layer of L. monocytogenes cells externally, showing promise as a potential solution to this problem. PlyP100, from the GRAS Listeria phage P100, is one such endolysin that can prevent the growth of L. monocytogenes in both lab culture conditions and a miniaturized queso fresco model. In this work, we aimed to understand the structural and functional properties of PlyP100. An AlphaFold prediction suggested the presence of three separate domains (D1, D2, and D3). By solving a crystal structure of D1 and assessing various domain truncations, we present evidence that D1 is responsible for catalytic activity, D3 is sufficient for cell wall binding, and D2 is necessary for full function of the enzyme against live cells. Additionally, we performed point mutations in D1 and compared PlyP100 to proteins with similar structures, including S. pneumoniae LytA and Listeria endolysin Ply511, in order to understand its specific enzymatic mechanism and target strain specificity. These insights into the structure and function of PlyP100 will aid future work aiming to engineer better endolysins as safe food antimicrobials. PubMed: 40441534DOI: 10.1016/j.jbc.2025.110295 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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