期刊
STRUCTURE
卷 25, 期 7, 页码 988-+出版社
CELL PRESS
DOI: 10.1016/j.str.2017.05.004
关键词
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资金
- MC CIG [303636]
- ISF [176/16]
- I-CORE Program of the Planning and Budgeting Committee [1775/12]
- Israel Science Foundation
- Edmond J. Safra Center for Bioinformatics at Tel Aviv University
- Israel Science Foundation [564/12]
CueR (Cu export regulator) is a metalloregulator protein that senses'' Cu(I) ions with very high affinity, thereby stimulating DNA binding and the transcription activation of two other metalloregulator proteins. The crystal structures of CueR when unbound or bound to DNA and a metal ion are very similar to each other, and the role of CueR and Cu(I) in initiating the transcription has not been fully understood yet. Using double electron-electron resonance (DEER) measurements and structure modeling, we investigate the conformational changes that CueR undergoes upon binding Cu(I) and DNA in solution. We observe three distinct conformations, corresponding to apo-CueR, DNA-bound CueR in the absence of Cu(I) (the repression'' state), and CueR-Cu(I)-DNA (the activation'' state). We propose a detailed structural mechanism underlying CueR's regulation of the transcription process. The mechanism explicitly shows the dependence of CueR activity on copper, thereby revealing the important negative feedback mechanism essential for regulating the intracellular copper concentration.
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