Structure of the effector-binding domain of deoxyribonucleoside regulator DeoR from Bacillus subtilis
Language English Country England, Great Britain Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
24863636
DOI
10.1111/febs.12856
Knihovny.cz E-resources
- Keywords
- Schiff base, X-ray crystallography, dimeric interface, effector binding, transcription repressor,
- MeSH
- Bacillus subtilis * MeSH
- Bacterial Proteins chemistry genetics MeSH
- Crystallography, X-Ray MeSH
- Protein Structure, Quaternary MeSH
- Models, Molecular MeSH
- Protein Multimerization MeSH
- Mutagenesis, Site-Directed MeSH
- Repressor Proteins chemistry genetics MeSH
- Solutions MeSH
- Schiff Bases chemistry MeSH
- Protein Structure, Secondary MeSH
- Amino Acid Sequence MeSH
- Structural Homology, Protein MeSH
- Amino Acid Substitution MeSH
- Protein Structure, Tertiary MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Hydrogen Bonding MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Bacterial Proteins MeSH
- Repressor Proteins MeSH
- Solutions MeSH
- Schiff Bases MeSH
UNLABELLED: 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. DATABASES: Atomic coordinates and structure factors for crystal structures of free C-DeoR and the covalent Schiff base complex of C-DeoR with dR5P have been deposited in the Protein Data Bank with accession codes 4OQQ and 4OQP, respectively. STRUCTURED DIGITAL ABSTRACT: C-DeoR and C-DeoR bind by x-ray crystallography (View interaction) DeoR and DeoR bind by molecular sieving (1, 2).
References provided by Crossref.org
Structure and function of bacterial transcription regulators of the SorC family
PDB
4OQP, 4OQQ
