4oqp

Publication Abstract from PubMed

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 mechanism of DeoR function as a molecular switch. This article is protected by copyright. All rights reserved.

Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis.,Skerlova J, Fabry M, Hubalek M, Otwinowski Z, Rezacova P FEBS J. 2014 May 23. doi: 10.1111/febs.12856. PMID:24863636^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.