6D6L
The structure of ligand binding domain of LasR in complex with TP-1 homolog, compound 14
Summary for 6D6L
| Entry DOI | 10.2210/pdb6d6l/pdb |
| Related | 6D6A 6D6B 6D6C 6D6D |
| Descriptor | Transcriptional activator protein LasR, 2,4-dibromo-6-{[(2-nitrobenzene-1-carbonyl)amino]methyl}phenyl 4-chlorobenzoate (3 entities in total) |
| Functional Keywords | luxr receptor, signaling protein, signaling protein-agonist complex, signaling protein/agonist |
| Biological source | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Total number of polymer chains | 4 |
| Total formula weight | 78308.27 |
| Authors | Dong, S.H.,Nair, S.K. (deposition date: 2018-04-21, release date: 2018-08-08, Last modification date: 2024-03-13) |
| Primary citation | O'Reilly, M.C.,Dong, S.H.,Rossi, F.M.,Karlen, K.M.,Kumar, R.S.,Nair, S.K.,Blackwell, H.E. Structural and Biochemical Studies of Non-native Agonists of the LasR Quorum-Sensing Receptor Reveal an L3 Loop "Out" Conformation for LasR. Cell Chem Biol, 25:1128-1139.e3, 2018 Cited by PubMed Abstract: Chemical strategies to block quorum sensing (QS) could provide a route to attenuate virulence in bacterial pathogens. Considerable research has focused on this approach in Pseudomonas aeruginosa, which uses the LuxR-type receptor LasR to regulate much of its QS network. Non-native ligands that antagonize LasR have been developed, yet we have little understanding of the mode by which these compounds interact with LasR and alter its function, as the receptor is unstable in their presence. Herein, we report an approach to circumvent this challenge through the study of a series of synthetic LasR agonists with varying levels of potency. Structural investigations of these ligands with the LasR ligand-binding domain reveal that certain agonists can enforce a conformation that deviates from that observed for other, often more potent agonists. These results, when combined with cell-based and biophysical analyses, suggest a functional model for LasR that could guide future ligand design. PubMed: 30033130DOI: 10.1016/j.chembiol.2018.06.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.63 Å) |
Structure validation
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