Structural and functional properties of antimicrobial protein L5 of Lysоbacter sp. XL1
The Gram-negative bacterium Lysobacter sp. XL1 secretes into the extracellular space five bacteriolytic enzymes that lyse the cell walls of competing microorganisms. Of special interest are homologous lytic proteases L1 and L5. This work found protein L5 to possess Gly-Gly endopeptidase and N-acetylmuramoyl-l-Ala amidase activities with respect to staphylococcal peptidoglycan. Protein L5 was found to be capable of aggregating into amyloid-like fibril structures. The crystal structure of protein L5 was determined at a 1.60-Å resolution. Protein L5 was shown to have a rather high structural identity with bacteriolytic protease L1 of Lysobacter sp. XL1 and α-lytic protease of Lysobacter enzymogenes at a rather low identity of their amino acid sequences. Still, the structure of protein L5 was revealed to have regions that differed from their equivalents in the homologs. The revealed structural distinctions in L5 are suggested to be of importance in exhibiting its unique properties.
KeywordsAntimicrobial proteins Bacteriolytic protease L5 Lysobacter sp. XL1 Peptidoglycan Substrate specificity Crystal structure of protein L5
We are grateful to Victor Selivanov for the English translation and Andrey Machulin and Vitaly Balobanov for the fruitful discussions.
The structural part of the study was supported by the program of the Presidium of the Russian Academy of Sciences “Molecular and Cell Biology and Postgenomic Technologies”. Electron-microscopic studies were carried out with the support of the Core Facility “UNIQEM Collection”, S.N. Winogradsky Institute of Microbiology, Research Center of Biotechnology, Russian Academy of Sciences.
Compliance with ethical standards
Conflict of interest
The authors declare that they have no conflict of interest.
The present study does not contain any experiments in relation to either human participants or animal models by any of the authors.
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