4HQM
The crystal structure of QsrR-menadione complex
Summary for 4HQM
| Entry DOI | 10.2210/pdb4hqm/pdb |
| Descriptor | QsrR protein, 2-methylnaphthalene-1,4-diol (2 entities in total) |
| Functional Keywords | menadione-modified protein, dna, transcription regulator |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 2 |
| Total formula weight | 26492.33 |
| Authors | Ji, Q.,Zhang, L.,Jones, M.B.,Sun, F.,Deng, X.,Liang, H.,Brugarolas, P.,Gao, N.,Peterson, S.N.,Lan, L.,Bae, T.,He, C. (deposition date: 2012-10-25, release date: 2013-03-06, Last modification date: 2024-11-20) |
| Primary citation | Ji, Q.,Zhang, L.,Jones, M.B.,Sun, F.,Deng, X.,Liang, H.,Cho, H.,Brugarolas, P.,Gao, Y.N.,Peterson, S.N.,Lan, L.,Bae, T.,He, C. Molecular mechanism of quinone signaling mediated through S-quinonization of a YodB family repressor QsrR. Proc.Natl.Acad.Sci.USA, 110:5010-5015, 2013 Cited by PubMed Abstract: Quinone 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° rigid-body rotation as well as a 9-Å 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. PubMed: 23479646DOI: 10.1073/pnas.1219446110 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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