6I56

Crystal structure of PBSX exported protein XepA

Summary for 6I56

• Entry DOI: 10.2210/pdb6i56/pdb
• Descriptor: Phage-like element PBSX protein XepA, GLYCEROL (3 entities in total)
• Functional Keywords: xepa, pbsx exported protein, xkdy, p31, unknown function
• Biological source: Bacillus subtilis subsp. subtilis str. 168
• Total number of polymer chains: 5
• Total formula weight: 152443.16

Authors

Hakansson, M.,Svensson, L.A.,Welin, M.,Al-Karadaghi, S. (deposition date: 2018-11-13, release date: 2019-11-20, Last modification date: 2024-05-15)

Primary citation

Freitag-Pohl, S.,Jasilionis, A.,Hakansson, M.,Svensson, L.A.,Kovacic, R.,Welin, M.,Watzlawick, H.,Wang, L.,Altenbuchner, J.,Plotka, M.,Kaczorowska, A.K.,Kaczorowski, T.,Nordberg Karlsson, E.,Al-Karadaghi, S.,Walse, B.,Aevarsson, A.,Pohl, E.
Crystal structures of the Bacillus subtilis prophage lytic cassette proteins XepA and YomS.
Acta Crystallogr D Struct Biol, 75:1028-1039, 2019

PubMed 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.

PubMed: 31692476
DOI: 10.1107/S2059798319013330

Experimental method

X-RAY DIFFRACTION (2.12 Å)