Acyldepsipeptide activated ClpP1P2 macromolecule of Leptospira, an ideal Achilles’ heel to hamper the cell survival and deregulate ClpP proteolytic activity
نویسندگان
چکیده
Antibiotic acyldepsipeptide (ADEP) targets the bacterial ClpP serine protease and can inhibit growth of numerous species by activating/dysregulating activity within cell. The spirochete Leptospira interrogans harbors two isoforms (LepClpP1 LepClpP2). Supplementation ADEP in medium resulted inhibition growth. mediated activation LepClpP mixture was dependent on time allowed for self-assembly LepClpP1 LepClpP2. dynamic light scattering presence indicated a conformational transformation machinery. Serine 98, catalytic triad residue LepClpP1P2 heterocomplex, critical activation. computational prototype structure suggested that hydrophobic pockets wherein ADEPs or physiological chaperone ClpX predominantly dock are exclusively present LepClpP2 heptamer. Using as tool, this investigation provides an insight into molecular function coalition with its ATPase LepClpX. shreds evidence illustrated verify ADEP1 possesses ability to control system unconventional approach than other organisms.
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ژورنال
عنوان ژورنال: Research in Microbiology
سال: 2021
ISSN: ['1769-7123', '0923-2508']
DOI: https://doi.org/10.1016/j.resmic.2021.103797