8TW1

Crystal structure of Lys2972, a phage endolysin targeting Streptococcus thermophilus

Summary for 8TW1

• Entry DOI: 10.2210/pdb8tw1/pdb
• Descriptor: Endolysin Lys2972, GLYCEROL, SODIUM ION, ... (4 entities in total)
• Functional Keywords: phage, endolysin, amidase, calcium-binding motif, hydrolase
• Biological source: Streptococcus phage 2972
• Total number of polymer chains: 1
• Total formula weight: 31933.85

Authors

Zhu, X.,Moineau, S.,Shi, R. (deposition date: 2023-08-18, release date: 2024-03-27, Last modification date: 2024-04-10)

Primary citation

Oechslin, F.,Zhu, X.,Morency, C.,Somerville, V.,Shi, R.,Moineau, S.
Fermentation Practices Select for Thermostable Endolysins in Phages.
Mol.Biol.Evol., 41:-, 2024

PubMed Abstract: Endolysins are produced by (bacterio)phages and play a crucial role in degrading the bacterial cell wall and the subsequent release of new phage progeny. These lytic enzymes exhibit a remarkable diversity, often occurring in a multimodular form that combines different catalytic and cell wall-binding domains, even in phages infecting the same species. Yet, our current understanding lacks insight into how environmental factors and ecological niches may have influenced the evolution of these enzymes. In this study, we focused on phages infecting Streptococcus thermophilus, as this bacterial species has a well-defined and narrow ecological niche, namely, dairy fermentation. Among the endolysins found in phages targeting this species, we observed limited diversity, with a singular structural type dominating in most of identified S. thermophilus phages. Within this prevailing endolysin type, we discovered a novel and highly conserved calcium-binding motif. This motif proved to be crucial for the stability and activity of the enzyme at elevated temperatures. Ultimately, we demonstrated its positive selection within the host's environmental conditions, particularly under the temperature profiles encountered in the production of yogurt, mozzarella, and hard cheeses that rely on S. thermophilus.

PubMed: 38489607
DOI: 10.1093/molbev/msae055

Experimental method

X-RAY DIFFRACTION (1.27 Å)