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Protein J. 2016 Feb;35(1):44-50. doi: 10.1007/s10930-015-9645-7.

Structural Studies of Component of Lysoamidase Bacteriolytic Complex from Lysobacter sp. XL1.

Author information

1
Institute of Protein Research, Russian Academy of Sciences, Institutskaya str. 4, Pushchino, 142290, Moscow Region, Russian Federation. sveta@vega.protres.ru.
2
Institute of Protein Research, Russian Academy of Sciences, Institutskaya str. 4, Pushchino, 142290, Moscow Region, Russian Federation.
3
G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Prospect Nauki 5, Pushchino, 142290, Moscow Region, Russian Federation.

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.

KEYWORDS:

Bacteriolytic protease L1; Circular dichroism; Crystals; Lysobacter sp. XL1; Structure; Thermal unfolding

PMID:
26717925
DOI:
10.1007/s10930-015-9645-7
[Indexed for MEDLINE]

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