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

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Bibliographic Details
Title: Crystal structures of the Bacillus subtilis prophage lytic cassette proteins XepA and YomS.
Authors: Freitag-Pohl, Stefanie, Jasilionis, Andrius, Håkansson, Maria, Svensson, Anders, Kovačič, Rebeka, Welin, Martin, Watzlawick, Hildegard, Wang, Lei, Altenbuchner, Josef, Plotka, Magdalena, Kaczorowska, Anna Karina, Kaczorowski, Tadeusz, Nordberg Karlsson, Eva, Al-Karadaghi, Salam, Walse, Bjorn, Aevarsson, Arnthor, Pohl, Ehmke
Source: Acta Crystallographica Section D: Structural Biology. 75:1028-1039
Subject Terms: Engineering and Technology, Industrial Biotechnology, Teknik, Industriell bioteknik
Description: 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 exhibitsdistinct 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.
Access URL: https://doi.org/10.1107/S2059798319013330
Database: SwePub
Description
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 exhibitsdistinct 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.
ISSN:20597983
DOI:10.1107/S2059798319013330