Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis

Jana Škerlová, Milan Fábry, Martin Hubálek, Zbyszek Otwinowski, Pavlína Řezáčová

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

Deoxyribonucleoside regulator (DeoR) from Bacillus subtilis negatively regulates expression of enzymes involved in the catabolism of deoxyribonucleosides and deoxyribose. The DeoR protein is homologous to the sorbitol operon regulator family of metabolic regulators and comprises an N-terminal DNA-binding domain and a C-terminal effector-binding domain. We have determined the crystal structure of the effector-binding domain of DeoR (C-DeoR) in free form and in covalent complex with its effector deoxyribose-5-phosphate (dR5P). This is the first case of a covalently attached effector molecule captured in the structure of a bacterial transcriptional regulator. The dR5P molecule is attached through a Schiff base linkage to residue Lys141. The crucial role of Lys141 in effector binding was confirmed by mutational analysis and mass spectrometry of Schiff base adducts formed in solution. Structural analyses of the free and effector-bound C-DeoR structures provided a structural explanation for the mechanism of DeoR function as a molecular switch.

Original languageEnglish (US)
Pages (from-to)4280-4292
Number of pages13
JournalFEBS Journal
Volume281
Issue number18
DOIs
StatePublished - Sep 1 2014

Keywords

  • Schiff base
  • X-ray crystallography
  • dimeric interface
  • effector binding
  • transcription repressor

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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