4OQP

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

4OQP の概要

• エントリーDOI: 10.2210/pdb4oqp/pdb
• 関連するPDBエントリー: 4OQQ
• 分子名称: Deoxyribonucleoside regulator, PENTANE-3,4-DIOL-5-PHOSPHATE, CADMIUM ION, ... (7 entities in total)
• 機能のキーワード: rossmann fold, sugar-binding transcriptional regulator, schiff base, transcription
• 由来する生物種: Bacillus subtilis subsp. subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29943.30

構造登録者

Rezacova, P.,Skerlova, J. (登録日: 2014-02-10, 公開日: 2014-06-04, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.6 Å)