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

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

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Circular Dichroism
  • Lysobacter / enzymology*
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Hydrolases / chemistry*
  • Peptide Hydrolases / metabolism*
  • Protein Unfolding

Substances

  • lysoamidase
  • Peptide Hydrolases