Chemical shift assignments of the catalytic domain of Staphylococcus aureus LytM
Tossavainen, H., Pitkänen, I., Antenucci, L., Thapa, C., & Permi, P. (2023). Chemical shift assignments of the catalytic domain of Staphylococcus aureus LytM. Biomolecular NMR Assignments, Early online. https://doi.org/10.1007/s12104-023-10161-3
Julkaistu sarjassa
Biomolecular NMR AssignmentsPäivämäärä
2023Oppiaine
Solu- ja molekyylibiologiaBiologisten vuorovaikutusten huippututkimusyksikköNanoscience CenterHyvinvoinnin tutkimuksen yhteisöCell and Molecular BiologyCentre of Excellence in Biological Interactions ResearchNanoscience CenterSchool of WellbeingTekijänoikeudet
© The Author(s) 2023
S. aureus resistance to antibiotics has increased rapidly. MRSA strains can simultaneously be resistant to many different classes of antibiotics, including the so-called “last-resort” drugs. Resistance complicates treatment, increases mortality and substantially increases the cost of treatment. The need for new drugs against (multi)resistant S. aureus is high. M23B family peptidoglycan hydrolases, enzymes that can kill S. aureus by cleaving glycine-glycine peptide bonds in S. aureus cell wall are attractive targets for drug development because of their binding specificity and lytic activity. M23B enzymes lysostaphin, LytU and LytM have closely similar catalytic domain structures. They however differ in their lytic activities, which can arise from non-conserved residues in the catalytic groove and surrounding loops or differences in dynamics. We report here the near complete 1 H/13C/15N resonance assignment of the catalytic domain of LytM, residues 185–316. The chemical shift data allow comparative structural and functional studies between the enzymes and is essential for understanding how these hydrolases degrade the cell wall.
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SpringerISSN Hae Julkaisufoorumista
1874-2718Asiasanat
Julkaisu tutkimustietojärjestelmässä
https://converis.jyu.fi/converis/portal/detail/Publication/194299398
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This work was supported by the grants from the Academy of Finland (number 323435) and Jane ja Aatos Erkon Säätiö. Open Access funding provided by University of Jyväskylä (JYU).Lisenssi
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