| Literature DB >> 26717925 |
Svetlana Tishchenko1, Azat Gabdulkhakov2, Bogdan Melnik2, Irina Kudryakova3, Oleg Latypov3, Natalya Vasilyeva3, Alexey Leontievsky3.
Abstract
The lysoamidase bacteriolytic complex (LBC) comprising five enzymes (L1-L5) is secreted into the culture liquid by gram-negative bacterium Lysobacter sp. XL1. The medicinal agent lysoamidase has a broad-antimicrobial spectrum. Bacteriolytic protease L1 belongs to the LBC. Recombinant L1 protease of Lysobacter sp. XL1 was expressed, purified to homogeneity and crystallized. The X-ray structure of L1 at 1.35 Å resolution has been determined using the synchrotron data and the molecular replacement method. L1 protease is a thermostable whose thermal unfolding proceeds in one step without forming stable intermediates. Structural information concerning L1 will contribute to the development of new-generation antimicrobial drugs, whose application will not be accompanied by the selection of resistant microorganisms.Entities:
Keywords: Bacteriolytic protease L1; Circular dichroism; Crystals; Lysobacter sp. XL1; Structure; Thermal unfolding
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Year: 2016 PMID: 26717925 DOI: 10.1007/s10930-015-9645-7
Source DB: PubMed Journal: Protein J ISSN: 1572-3887 Impact factor: 2.371