4ZA6
Structure of the R. erythropolis transcriptional repressor QsdR from TetR family
Summary for 4ZA6
| Entry DOI | 10.2210/pdb4za6/pdb |
| Descriptor | TetR family transcriptional regulator, (4S)-2-METHYL-2,4-PENTANEDIOL, ACETATE ION, ... (5 entities in total) |
| Functional Keywords | quorum-sensing, nahl degradation, qsda transcriptional regulator, rhodococcus erythropolis r138, signaling protein |
| Biological source | Rhodococcus erythropolis |
| Total number of polymer chains | 2 |
| Total formula weight | 43508.38 |
| Authors | El Sahili, A.,Morera, S. (deposition date: 2015-04-13, release date: 2015-10-21, Last modification date: 2024-05-01) |
| Primary citation | El Sahili, A.,Kwasiborski, A.,Mothe, N.,Velours, C.,Legrand, P.,Morera, S.,Faure, D. Natural Guided Genome Engineering Reveals Transcriptional Regulators Controlling Quorum-Sensing Signal Degradation. Plos One, 10:e0141718-e0141718, 2015 Cited by PubMed Abstract: Quorum-quenching (QQ) are natural or engineered processes disrupting the quorum-sensing (QS) signalling which controls virulence and persistence (e.g. biofilm) in numerous bacteria. QQ involves different enzymes including lactonases, amidases, oxidases and reductases which degrade the QS molecules such as N-acylhomoserine lactones (NAHL). Rhodococcus erythropolis known to efficiently degrade NAHL is proposed as a biocontrol agent and a reservoir of QQ-enzymes for biotechnology. In R. erythropolis, regulation of QQ-enzymes remains unclear. In this work, we performed genome engineering on R. erythropolis, which is recalcitrant to reverse genetics, in order to investigate regulation of QQ-enzymes at a molecular and structural level with the aim to improve the QQ activity. Deep-sequencing of the R. erythropolis enhanced variants allowed identification of a punctual mutation in a key-transcriptional factor QsdR (Quorum sensing degradation Regulation) which regulates the sole QQ-lactonase QsdA identified so far. Using biophysical and structural studies on QsdR, we demonstrate that QQ activity can be improved by modifying the regulation of QQ-enzymes degrading QS signal. This modification requiring the change of only one amino-acid in a transcriptional factor leads to an enhanced R. erythropolis in which the QS-signal degradation pathway is strongly activated. PubMed: 26554837DOI: 10.1371/journal.pone.0141718 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.97 Å) |
Structure validation
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