Crystal structures of the Bacillus subtilis prophage lytic cassette proteins XepA and YomS

Freitag-Pohl, S.; Jasilionis, A.; Håkansson, M.; Svensson, L.A.; Kovačič, R.; Welin, M.; Watzlawick, H.; Wang, L.; Altenbuchner, J.; Płotka, M.; Kaczorowska, A.K.; Kaczorowski, T.; Nordberg Karlsson, E.; Al-Karadaghi, S.; Walse, B.; Aevarsson, A.; Pohl, E.

doi:10.1107/S2059798319013330

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 8
Cytotoxicity of target enzymes. Bacterial plate assays of XepA, YomS, XlyA and XlyB. HEWL and HEPES buffer (20 mM, pH 7.4) were used as positive and negative controls, respectively. (a) B. megaterium ATCC 14581, (b) B. subtilis subsp. spizizenii ATCC 6633, (c) B. pumilus KPD 181, (d) B. thuringiensis KPD 114, (e) B. mycoides KPD 15, (f) M. luteus ATCC 4698, (g) E. coli MG 1655, (h) B. subtilis 168 DSM 23778. The activities of the following proteins were also tested: the YeaH protein of unknown function from B. subtilis and PGN hydrolase, a putative lytic enzyme from B. subtilis phage vB_BsuP-Goe1.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 75| Part 11| November 2019| Pages 1028-1039

https://doi.org/10.1107/S2059798319013330

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