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

DOI: 10.1107/S2059798319013330 DOI Help

Authors: Stefanie Freitag-pohl (Durham University) , Andrius Jasilionis (Durham University) , Maria Håkansson (SARomics Biostructures) , L. Anders Svensson (SARomics Biostructures) , Rebeka Kovačič (SARomics Biostructures) , Martin Welin (SARomics Biostructures) , Hildegard Watzlawick (University of Stuttgart) , Lei Wang (University of Stuttgart) , Josef Altenbuchner (University of Stuttgart) , Magdalena Płotka (University of Gdańsk) , Anna Karina Kaczorowska (University of Gdańsk) , Tadeusz Kaczorowski (University of Gdańsk) , Eva Nordberg Karlsson (Lund University) , Salam Al-karadaghi (SARomics Biostructures) , Björn Walse (SARomics Biostructures) , Arnthór Aevarsson (Matis) , Ehmke Pohl (Durham University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section D Structural Biology , VOL 75 , PAGES 1028 - 1039

State: Published (Approved)
Published: November 2019

Abstract: As part of the Virus-X Consortium that aims to identify and characterize novel proteins and enzymes from bacteriophages and archaeal viruses, the genes of the putative lytic proteins XepA from Bacillus subtilis prophage PBSX and YomS from prophage SPβ were cloned and the proteins were subsequently produced and functionally characterized. In order to elucidate the role and the molecular mechanism of XepA and YomS, the crystal structures of these proteins were solved at resolutions of 1.9 and 1.3 Å, respectively. XepA consists of two antiparallel β-sandwich domains connected by a 30-amino-acid linker region. A pentamer of this protein adopts a unique dumbbell-shaped architecture consisting of two discs and a central tunnel. YomS (12.9 kDa per monomer), which is less than half the size of XepA (30.3 kDa), shows homology to the C-terminal part of XepA and exhibits a similar pentameric disc arrangement. Each β-sandwich entity resembles the fold of typical cytoplasmic membrane-binding C2 domains. Only XepA exhibits distinct cytotoxic activity in vivo, suggesting that the N-terminal pentameric domain is essential for this biological activity. The biological and structural data presented here suggest that XepA disrupts the proton motive force of the cytoplasmatic membrane, thus supporting cell lysis.

Journal Keywords: prophage; Virus-X Consortium; lytic enzymes; lytic cassette proteins; Bacillus subtilis; XepA; YomS

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

Other Facilities: DESY