Insights into Protein Allostery in the CsoR/RcnR Family of Transcriptional Repressors | Zendy

Khadine A. Higgins | Zendy; David Giedroc | Zendy

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Insights into Protein Allostery in the CsoR/RcnR Family of Transcriptional Repressors

Author(s) -

Khadine A. Higgins,

David Giedroc

Publication year - 2013

Publication title -

chemistry letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.492

H-Index - 114

eISSN - 1348-0715

pISSN - 0366-7022

DOI - 10.1246/cl.130965

Subject(s) - repressor , chemistry , dimer , allosteric regulation , cysteine , biochemistry , gene , stereochemistry , computational biology , genetics , transcription factor , biology , enzyme , organic chemistry

CsoR/RcnR transcriptional repressors adopt a disc-shaped, all α-helical dimer of dimers tetrameric architecture, with a four-helix bundle the key structural feature of the dimer. Individual members of this large family of repressors coordinate Cu(I) or Ni(II)/Co(II) or perform cysteine sulfur chemistry in mitigating the effects of metal or metabolite toxicity, respectively. Here we highlight recent insights into the functional diversity of this fascinating family of repressors.

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