4OQP

Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis in complex with deoxyribose-5-phosphate

Summary for 4OQP

• Entry DOI: 10.2210/pdb4oqp/pdb
• Related: 4OQQ
• Descriptor: Deoxyribonucleoside regulator, PENTANE-3,4-DIOL-5-PHOSPHATE, CADMIUM ION, ... (7 entities in total)
• Functional Keywords: rossmann fold, sugar-binding transcriptional regulator, schiff base, transcription
• Biological source: Bacillus subtilis subsp. subtilis
• Total number of polymer chains: 1
• Total formula weight: 29943.30

Authors

Rezacova, P.,Skerlova, J. (deposition date: 2014-02-10, release date: 2014-06-04, Last modification date: 2024-11-06)

Primary citation

Skerlova, J.,Fabry, M.,Hubalek, M.,Otwinowski, Z.,Rezacova, P.
Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis.
Febs J., 281:4280-4292, 2014

PubMed 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.

PubMed: 24863636
DOI: 10.1111/febs.12856

Experimental method

X-RAY DIFFRACTION (1.6 Å)