Structural Studies of Component of Lysoamidase Bacteriolytic Complex from Lysobacter sp. XL1
Svetlana Tishchenko1, Azat Gabdulkhakov2, Bogdan Melnik2
1Institute of Protein Research, Russian Academy of Sciences, Institutskaya str. 4, Pushchino, 142290, Moscow Region, Russian Federation. sveta@vega.protres.ru.
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.
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