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The crystal structure of QsrR-DNA complexThe crystal structure of QsrR-DNA complex
Structural highlights
FunctionPublication Abstract from PubMedQuinone molecules are intracellular electron-transport carriers, as well as critical intra- and extracellular signals. However, transcriptional regulation of quinone signaling and its molecular basis are poorly understood. Here, we identify a thiol-stress-sensing regulator YodB family transcriptional regulator as a central component of quinone stress response of Staphylococcus aureus, which we have termed the quinone-sensing and response repressor (QsrR). We also identify and confirm an unprecedented quinone-sensing mechanism based on the S-quinonization of the essential residue Cys-5. Structural characterizations of the QsrR-DNA and QsrR-menadione complexes further reveal that the covalent association of menadione directly leads to the release of QsrR from operator DNA following a 10 degrees rigid-body rotation as well as a 9-A elongation between the dimeric subunits. The molecular level characterization of this quinone-sensing transcriptional regulator provides critical insights into quinone-mediated gene regulation in human pathogens. Molecular mechanism of quinone signaling mediated through S-quinonization of a YodB family repressor QsrR.,Ji Q, Zhang L, Jones MB, Sun F, Deng X, Liang H, Cho H, Brugarolas P, Gao YN, Peterson SN, Lan L, Bae T, He C Proc Natl Acad Sci U S A. 2013 Mar 26;110(13):5010-5. doi:, 10.1073/pnas.1219446110. Epub 2013 Mar 11. PMID:23479646[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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