Paweł Mitkowski
International Institute of Minnesota
4 Papers
4 Citations
Paweł Mitkowski is an academic researcher from International Institute of Minnesota. The author has contributed to research in topics: Peptidoglycan & Gene. The author has an hindex of 1, co-authored 2 publications.
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Papers
One fold, many functions—M23 family of peptidoglycan hydrolases
TL;DR: This work systematizes the knowledge of the M23 family enzymes in the context of their unique antimicrobial potential against drug-resistant pathogens and presents possibilities to modulate and engineer their features to develop perfect antibacterial weapons.
Structural Characterization of EnpA D,L-Endopeptidase from Enterococcus faecalis Prophage Provides Insights into Substrate Specificity of M23 Peptidases
Piotr H. Malecki,Paweł Mitkowski,Elżbieta Jagielska,Karolina Trochimiak,Stéphane Mesnage,Izabela Sabala +5 more
TL;DR: In this paper, a detailed analysis of the binding groove architecture, specificity of EnpACD enzymes and D,L peptidases demonstrates that the substrate groove, which is particularly deep and narrow, is accessible for peptides composed of amino acids with short side chains or subsequent L and D-isomers.
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Enhancing stability and safety of chimeric peptidoglycan hydrolases by linker engineering
Paweł Mitkowski,Elżbieta Jagielska,Małgorzata Korzeniowska nee Wiweger,Marzena Nowacka,Morten Kjos,Christian Kranjec,Izabela Sabala +6 more
TL;DR: Engineers linkers to enhance stability and safety of chimeric peptidoglycan hydrolases, creating efficient, safe, and stable enzybiotics that eliminate E. faecalis and S. aureus without cytotoxic effects or resistance development.
Structural bases of peptidoglycan recognition by lysostaphin SH3b domain
Paweł Mitkowski,Elżbieta Jagielska,Elzbieta Nowak,Janusz M. Bujnicki,Janusz M. Bujnicki,Filip Stefaniak,Dorota Niedzialek,Matthias Bochtler,Matthias Bochtler,Izabela Sabała +9 more
TL;DR: The structure suggests that pentaglycine specificity of the SH3b arises partially directly by steric exclusion of Cβ atoms in the ligand and partially indirectly due to the selection of main chain conformations that are easily accessible for glycine, but not other amino acid residues.