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8EZR

Crystal structure of the HipS(Lp)-HipT(Lp) complex from Legionella pneumophila, native protein

Summary for 8EZR
Entry DOI10.2210/pdb8ezr/pdb
DescriptorHipS(Lp), HipT(Lp), DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
Functional Keywordstoxin-antitoxin complex, legionella pneumophila, structural genomics, center for structural genomics of infectious diseases, csgid, national institute of allergy and infectious diseases, niaid, toxin
Biological sourceLegionella pneumophila
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Total number of polymer chains2
Total formula weight47838.68
Authors
Primary citationLin, J.D.,Stogios, P.J.,Abe, K.T.,Wang, A.,MacPherson, J.,Skarina, T.,Gingras, A.-.C.,Savchenko, A.,Ensminger, A.W.
Functional diversification despite structural congruence in the HipBST toxin-antitoxin system of Legionella pneumophila.
Mbio, 14:e0151023-e0151023, 2023
Cited by
PubMed Abstract: Toxin-antitoxin (TA) systems are parasitic genetic elements found in almost all bacterial genomes. They are exchanged horizontally between cells and are typically poorly conserved across closely related strains and species. Here, we report the characterization of a tripartite TA system in the bacterial pathogen that is highly conserved across species genomes. This system (denoted HipBST) is a distant homolog of the recently discovered split-HipA system in (HipBST). We present bioinformatic, molecular, and structural analyses of the divergence between these two systems and the functionality of this newly described TA system family. Furthermore, we provide evidence to refute previous claims that the toxin in this system (HipT) possesses bifunctionality as an virulence protein. Overall, this work expands our understanding of the split-HipA system architecture and illustrates the potential for undiscovered biology in these abundant genetic elements.
PubMed: 37819088
DOI: 10.1128/mbio.01510-23
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

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