8EZR
Crystal structure of the HipS(Lp)-HipT(Lp) complex from Legionella pneumophila, native protein
Summary for 8EZR
| Entry DOI | 10.2210/pdb8ezr/pdb |
| Descriptor | HipS(Lp), HipT(Lp), DI(HYDROXYETHYL)ETHER, ... (5 entities in total) |
| Functional Keywords | toxin-antitoxin complex, legionella pneumophila, structural genomics, center for structural genomics of infectious diseases, csgid, national institute of allergy and infectious diseases, niaid, toxin |
| Biological source | Legionella pneumophila More |
| Total number of polymer chains | 2 |
| Total formula weight | 47838.68 |
| Authors | Stogios, P.J.,Skarina, T.,Michalska, K.,Di Leo, R.,Lin, J.,Ensminger, A.,Savchenko, A.,Joachimiak, A.,Satchell, K.J.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2022-11-01, release date: 2023-09-27, Last modification date: 2026-02-25) |
| Primary citation | Lin, 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: 37819088DOI: 10.1128/mbio.01510-23 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
Download full validation report






