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

Freitag-Pohl, Stefanie ; Jasilionis, Andrius LU ; Håkansson, Maria ; Svensson, Anders ; Kovačič, Rebeka ; Welin, Martin LU ; Watzlawick, Hildegard ; Wang, Lei ; Altenbuchner, Josef and Plotka, Magdalena , et al. (2019) In Acta Crystallographica Section D: Structural Biology 75. p.1028-1039
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... (More)
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. (Less)
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Acta Crystallographica Section D: Structural Biology
volume
75
pages
1028 - 1039
publisher
John Wiley & Sons Inc.
external identifiers
  • scopus:85074584812
  • pmid:31692476
ISSN
2059-7983
DOI
10.1107/S2059798319013330
language
English
LU publication?
yes
id
abfab77d-eebb-46fc-8551-3aa19500ccfc
date added to LUP
2019-10-06 19:31:48
date last changed
2023-07-03 09:43:29
@article{abfab77d-eebb-46fc-8551-3aa19500ccfc,
  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.}},
  author       = {{Freitag-Pohl, Stefanie and Jasilionis, Andrius and Håkansson, Maria and Svensson, Anders and Kovačič, Rebeka and Welin, Martin and Watzlawick, Hildegard and Wang, Lei and Altenbuchner, Josef and Plotka, Magdalena and Kaczorowska, Anna Karina and Kaczorowski, Tadeusz and Nordberg Karlsson, Eva and Al-Karadaghi, Salam and Walse, Bjorn and Aevarsson, Arnthor and Pohl, Ehmke}},
  issn         = {{2059-7983}},
  language     = {{eng}},
  month        = {{11}},
  pages        = {{1028--1039}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{Acta Crystallographica Section D: Structural Biology}},
  title        = {{Crystal structures of the Bacillus subtilis prophage lytic cassette proteins XepA and YomS.}},
  url          = {{http://dx.doi.org/10.1107/S2059798319013330}},
  doi          = {{10.1107/S2059798319013330}},
  volume       = {{75}},
  year         = {{2019}},
}