6SY9
Structure of the Legionella pneumophila response regulator LqsR
Summary for 6SY9
| Entry DOI | 10.2210/pdb6sy9/pdb |
| Descriptor | Response regulator (2 entities in total) |
| Functional Keywords | response regulator, receiver domain, output domain, signaling protein |
| Biological source | Legionella pneumophila |
| Total number of polymer chains | 1 |
| Total formula weight | 41493.84 |
| Authors | Hochstrasser, R.,Hutter, C.A.J.,Arnold, F.M.,Baerlocher, K.,Seeger, M.A.,Hilbi, H. (deposition date: 2019-09-27, release date: 2020-02-05, Last modification date: 2024-05-15) |
| Primary citation | Hochstrasser, R.,Hutter, C.A.J.,Arnold, F.M.,Barlocher, K.,Seeger, M.A.,Hilbi, H. The structure of the Legionella response regulator LqsR reveals amino acids critical for phosphorylation and dimerization. Mol.Microbiol., 113:1070-1084, 2020 Cited by PubMed Abstract: The water-borne bacterium Legionella pneumophila replicates in environmental protozoa and upon inhalation destroys alveolar macrophages, thus causing a potentially fatal pneumonia termed 'Legionnaires' disease'. L. pneumophila employs the Legionella quorum sensing (Lqs) system to control its life cycle, pathogen-host cell interactions, motility and natural competence. Signaling through the Lqs system occurs through the α-hydroxyketone compound Legionella autoinducer-1 (LAI-1) and converges on the prototypic response regulator LqsR, which dimerizes upon phosphorylation of the conserved aspartate, D . In this study, we determine the high-resolution structure of monomeric LqsR. The structure reveals a receiver domain adopting a canonical (βα) fold, which is connected through an additional sixth helix and an extended α5-helix to a novel output domain. The two domains delineate a mainly positively charged groove, and the output domain adopts a five-stranded antiparallel β-sheet fold similar to nucleotide-binding proteins. Structure-based mutagenesis identified amino acids critical for LqsR phosphorylation and dimerization. Upon phosphorylation, the LqsR and LqsR mutant proteins dimerized even more readily than wild-type LqsR, and no evidence for semi-phosphorylated heterodimers was obtained. Taken together, the high-resolution structure of LqsR reveals functionally relevant amino acid residues implicated in signal transduction of the prototypic response regulator. PubMed: 31997467DOI: 10.1111/mmi.14477 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
Download full validation report
