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

Stefanie Freitag-Pohl , Andrius Jasilionis , Maria Håkansson , L. Anders Svensson , Rebeka Kovačič , Martin Welin , Hildegard Watzlawick , Wang Lei , Josef Altenbuchner , Magdalena Płotka , Anna Kaczorowska , Tadeusz Kaczorowski , Eva Nordberg Karlsson , Salam Al-Karadaghi , Björn Walse , Arnthór Aevarsson , Ehmke Pohl

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 Stefanie Freitag-Pohl
Stefanie Freitag-Pohl,,
-
, Andrius Jasilionis
Andrius Jasilionis,,
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, Maria Håkansson
Maria Håkansson,,
-
, L. Anders Svensson
L. Anders Svensson,,
-
, Rebeka Kovačič
Rebeka Kovačič,,
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, Martin Welin
Martin Welin,,
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, Hildegard Watzlawick
Hildegard Watzlawick,,
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, Wang Lei
Wang Lei,,
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, Josef Altenbuchner
Josef Altenbuchner,,
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, Magdalena Płotka (FB/DM)
Magdalena Płotka,,
- Department of Microbiology
et al.`
Journal seriesActa Crystallographica Section D-Structural Biology, [Acta Crystallographica Section D: Structural Biology], ISSN 2059-7983, (N/A 100 pkt)
Issue year2019
Vol75
No11
Pages1028-1039
Publication size in sheets0.55
Keywords in Polishkonsorcjum Virus-X, enzymy lityczne, kasety białkowe, Bacillus subtilis
Keywords in Englishprophage, Virus-X Consortium, lytic enzymes, lytic cassette proteins, Bacillus subtilis, XepA, YomS
ASJC Classification1315 Structural Biology
DOIDOI:10.1107/S2059798319013330
Languageen angielski
LicenseRepository; published final; Uznanie Autorstwa (CC-BY); with publication
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Kaczorowski_Tadeusz_Crystal_structures_of_the_Bacillus_subtilis_2019.pdf Kaczorowski_Tadeusz_Crystal_structures_of_the_Bacillus_subtilis_2019.pdf 2,19 MB
Score (nominal)100
Score sourcejournalList
ScoreMinisterial score = 100.0, 10-02-2020, ArticleFromJournal
Publication indicators WoS Citations = 0.000; Scopus SNIP (Source Normalised Impact per Paper): 2018 = 1.111; WoS Impact Factor: 2018 = 3.227 (2) - 2018=3.020 (5)
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LicencjaUtwór jest udostępniany na licencji Creative Commons Uznanie autorstwa 4.0 Międzynarodowe (CC BY 4.0) https://creativecommons.org/licenses/by/4.0/
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