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4HQE

The crystal structure of QsrR-DNA complex

Summary for 4HQE
Entry DOI10.2210/pdb4hqe/pdb
DescriptorTranscriptional regulator QsrR, DNA (5'-D(*GP*GP*TP*AP*TP*AP*AP*TP*AP*AP*TP*TP*AP*TP*AP*CP*T)-3'), DNA (5'-D(*AP*GP*TP*AP*TP*AP*AP*TP*TP*AP*TP*TP*AP*TP*AP*CP*C)-3'), ... (4 entities in total)
Functional Keywordstranscriptional regulator, dna, transcription-dna complex, transcription/dna
Biological sourceStaphylococcus aureus
More
Total number of polymer chains4
Total formula weight36617.04
Authors
He, C.,Ji, Q.,Zhang, L. (deposition date: 2012-10-25, release date: 2013-03-06, Last modification date: 2024-02-28)
Primary citationJi, 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: 23479646
DOI: 10.1073/pnas.1219446110
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.299 Å)
Structure validation

237735

数据于2025-06-18公开中

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