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Appl Microbiol Biotechnol. 2018 Dec;102(23):10043-10053. doi: 10.1007/s00253-018-9364-z. Epub 2018 Sep 18.

Structural and functional properties of antimicrobial protein L5 of Lysоbacter sp. XL1.

Author information

1
G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 5 Pr. Nauki, Pushchino, Moscow Region, Russia, 142290.
2
Institute of Protein Research, Russian Academy of Sciences, 4 Institutskaya Str., Pushchino, Moscow Region, Russia, 142290.
3
G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 5 Pr. Nauki, Pushchino, Moscow Region, Russia, 142290. vasilyevanv@rambler.ru.

Abstract

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.

KEYWORDS:

Antimicrobial proteins; Bacteriolytic protease L5; Crystal structure of protein L5; Lysobacter sp. XL1; Peptidoglycan; Substrate specificity

PMID:
30229324
DOI:
10.1007/s00253-018-9364-z
[Indexed for MEDLINE]

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