8SSH
MtrR from Neisseria gonorrhoeae bound to Ethinyl Estradiol
Summary for 8SSH
| Entry DOI | 10.2210/pdb8ssh/pdb |
| Descriptor | HTH-type transcriptional regulator MtrR, Ethinyl estradiol, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | hth, regulator, hormone, induction, transcription |
| Biological source | Neisseria gonorrhoeae |
| Total number of polymer chains | 4 |
| Total formula weight | 99763.40 |
| Authors | Hooks, G.M.,Brennan, R.G. (deposition date: 2023-05-08, release date: 2024-02-14, Last modification date: 2024-04-03) |
| Primary citation | Hooks, G.M.,Ayala, J.C.,Holley, C.L.,Dhulipala, V.,Beggs, G.A.,Perfect, J.R.,Schumacher, M.A.,Shafer, W.M.,Brennan, R.G. Hormonal steroids induce multidrug resistance and stress response genes in Neisseria gonorrhoeae by binding to MtrR. Nat Commun, 15:1153-1153, 2024 Cited by PubMed Abstract: Transcriptional regulator MtrR inhibits the expression of the multidrug efflux pump operon mtrCDE in the pathogenic bacterium Neisseria gonorrhoeae. Here, we show that MtrR binds the hormonal steroids progesterone, β-estradiol, and testosterone, which are present at urogenital infection sites, as well as ethinyl estrogen, a component of some hormonal contraceptives. Steroid binding leads to the decreased affinity of MtrR for cognate DNA, increased mtrCDE expression, and enhanced antimicrobial resistance. Furthermore, we solve crystal structures of MtrR bound to each steroid, thus revealing their binding mechanisms and the conformational changes that induce MtrR. PubMed: 38326294DOI: 10.1038/s41467-024-45195-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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