• Korean Journal of Food Science and Technology
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• v.48 no.6
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• pp.560-564
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• 2016

The objective of this study was to investigate the anti-Bacillus cereus activity of actinonin. Actinonin inhibited the growth of B. cereus in a dose dependent manner. The growth-inhibitory activity of actinonin was evaluated using a broth micro-dilution method, and minimum inhibitory concentration (MIC) and agar disk diffusion tests. B. cereus showed high susceptibility to actinonin in a concentration-dependent manner and MIC was determined to be $0.192{\mu}g/mL$. Additionally, 1 and 2 mM actinonin induced formation of B. cereus inhibition zones. In addition, as compared to B. cereus alone, B. cereus added with $10{\mu}M$ actinonin showed a lower level of cytotoxicity in HeLa cells in vitro. Thus, this study revealed that actinonin could be a potential source of a natural antimicrobial agent or a pharmaceutical component against B. cereus.

• BMB Reports
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• v.40 no.6
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• pp.1050-1057
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• 2007

Peptide deformylase (PDF) is a metalloenzyme that removes the N-terminal formyl groups from newly synthesized proteins. It is essential for bacterial survival, and is therefore-considered as a potential target for antimicrobial chemotherapy. However, some bacteria including medically relevant pathogens possess two or more def-like genes. Here we have examined two PDFs from Bacillus cereus. The two share only 32% sequence identity and the crystal structures show overall similarity with PDF2 having a longer C-terminus. However, there are differences at the two active sites, and these differences appear to contribute to the activity difference seen between the two. BcPDF2 is found as a dimer in the crystal form with two additional actinonin bound at that interface.

• Korean Journal of Crystallography
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• v.15 no.1
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• pp.40-43
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• 2004

The peptide deformylase from the pathogenic bacterium Staphylococcus aureus has been over-expressed in Escherichia coli and crystallized in the presence of the inhibitor actinonin at 297 K using polyethylene glycol 20000 as a precipitant. X-ray diffraction data have been collected to 2.2 ${\AA}$ resolution. The crystal is trigonal, belonging to the space group $P3_121$ (or its enantiomorph $P3_221$), with unit cell parameters of a = b = 62.70 ${\AA}$ c = 108.23 ${\AA}$, ${\alpha}\;=\;{\beta}\;=\;90^{\circ},\;and\;{\gamma}\;=\;120^{\circ}$. An asymmetric unit contains a monomer of the recombinant enzyme, giving a $V_M$ of 2.84 ${\AA}^3\;Da^_{-1}$ and a solvent content of 56.7%.