6i56

Crystal structure of PBSX exported protein XepA

spinqualitylabelsall models 6i56, resolution 2.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6i56 is a 5 chain structure with sequence from Bacsu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL Gene: xepA, xkdY, BSU12780 (BACSU) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [XEPA_BACSU] Not known; does not seem to be involved in host cell lysis. Publication Abstract from PubMed 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 SPbeta 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 A, respectively. XepA consists of two antiparallel beta-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 beta-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. Crystal structures of the Bacillus subtilis prophage lytic cassette proteins XepA and YomS.,Freitag-Pohl S, Jasilionis A, Hakansson M, Svensson LA, Kovacic R, Welin M, Watzlawick H, Wang L, Altenbuchner J, Plotka M, Kaczorowska AK, Kaczorowski T, Nordberg Karlsson E, Al-Karadaghi S, Walse B, Aevarsson A, Pohl E Acta Crystallogr D Struct Biol. 2019 Nov 1;75(Pt 11):1028-1039. doi:, 10.1107/S2059798319013330. Epub 2019 Nov 1. PMID:31692476 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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