8fw3
MtrR from Neisseria gonorrhoeae bound to Testosterone
Structural highlights
FunctionMTRR_NEIGO Controls the permeability of the cell envelope to hydrophobic compounds such as antibiotics and detergents (PubMed:8196548). Represses transcription of the mtrCDE-encoded efflux pump by binding within the mtrCDE promoter (PubMed:9209024, PubMed:23221802). Also negatively regulates the expression of farR, by binding to its promoter region, leading indirectly to the positive regulation of expression of the farAB-encoded efflux pump (PubMed:14645274).[1] [2] [3] [4] Publication Abstract from PubMedTranscriptional 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, beta-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. Hormonal steroids induce multidrug resistance and stress response genes in Neisseria gonorrhoeae by binding to MtrR.,Hooks GM, Ayala JC, Holley CL, Dhulipala V, Beggs GA, Perfect JR, Schumacher MA, Shafer WM, Brennan RG Nat Commun. 2024 Feb 7;15(1):1153. doi: 10.1038/s41467-024-45195-1. PMID:38326294[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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