3QP5
Crystal structure of CviR bound to antagonist chlorolactone (CL)
Summary for 3QP5
| Entry DOI | 10.2210/pdb3qp5/pdb |
| Related | 3QP1 3QP2 3QP4 3QP6 3QP7 3QP8 |
| Descriptor | CviR transcriptional regulator, 4-(4-chlorophenoxy)-N-[(3S)-2-oxotetrahydrofuran-3-yl]butanamide (2 entities in total) |
| Functional Keywords | quorum sensing, agonist, antagonist, luxr, acylated homoserine lactone, transcription factor, dna binding protein, ligand binding domain, signal receptor, quorum sensing transcription factor, chlorolactone (cl), transcription |
| Biological source | Chromobacterium violaceum |
| Total number of polymer chains | 4 |
| Total formula weight | 120203.01 |
| Authors | Chen, G.,Swem, L.,Swem, D.,Stauff, D.,O'Loughlin, C.,Jeffrey, P.,Bassler, B.,Hughson, F. (deposition date: 2011-02-11, release date: 2011-03-30, Last modification date: 2023-09-13) |
| Primary citation | Chen, G.,Swem, L.R.,Swem, D.L.,Stauff, D.L.,O'Loughlin, C.T.,Jeffrey, P.D.,Bassler, B.L.,Hughson, F.M. A strategy for antagonizing quorum sensing. Mol.Cell, 42:199-209, 2011 Cited by PubMed Abstract: Quorum-sensing bacteria communicate via small molecules called autoinducers to coordinate collective behaviors. Because quorum sensing controls virulence factor expression in many clinically relevant pathogens, membrane-permeable quorum sensing antagonists that prevent population-wide expression of virulence genes offer a potential route to novel antibacterial therapeutics. Here, we report a strategy for inhibiting quorum-sensing receptors of the widespread LuxR family. Structure-function studies with natural and synthetic ligands demonstrate that the dimeric LuxR-type transcription factor CviR from Chromobacterium violaceum is potently antagonized by molecules that bind in place of the native acylated homoserine lactone autoinducer, provided that they stabilize a closed conformation. In such conformations, each of the two DNA-binding domains interacts with the ligand-binding domain of the opposing monomer. Consequently, the DNA-binding helices are held apart by ∼60 Å, twice the ∼30 Å separation required for operator binding. This approach may represent a general strategy for the inhibition of multidomain proteins. PubMed: 21504831DOI: 10.1016/j.molcel.2011.04.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.249 Å) |
Structure validation
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