7BHY
DNA-binding domain of DeoR in complex with the DNA operator
Summary for 7BHY
| Entry DOI | 10.2210/pdb7bhy/pdb |
| Descriptor | DNA operator - strand 1, DNA operator - strand 2, Deoxyribonucleoside regulator, ... (5 entities in total) |
| Functional Keywords | transcriptional repressor, deoxyribose catabolism, helix-turn-helix domain, bacillus subtilis, dna binding protein |
| Biological source | Bacillus subtilis subsp. subtilis str. 168 More |
| Total number of polymer chains | 5 |
| Total formula weight | 29263.14 |
| Authors | Novakova, M.,Rezacova, P.,Skerlova, J.,Brynda, J. (deposition date: 2021-01-11, release date: 2021-11-10, Last modification date: 2024-01-31) |
| Primary citation | Soltysova, M.,Sieglova, I.,Fabry, M.,Brynda, J.,Skerlova, J.,Rezacova, P. Structural insight into DNA recognition by bacterial transcriptional regulators of the SorC/DeoR family. Acta Crystallogr D Struct Biol, 77:1411-1424, 2021 Cited by PubMed Abstract: The SorC/DeoR family is a large family of bacterial transcription regulators that are involved in the control of carbohydrate metabolism and quorum sensing. To understand the structural basis of DNA recognition, structural studies of two functionally characterized SorC/DeoR family members from Bacillus subtilis were performed: the deoxyribonucleoside regulator bsDeoR and the central glycolytic genes regulator bsCggR. Each selected protein represents one of the subgroups that are recognized within the family. Crystal structures were determined of the N-terminal DNA-binding domains of bsDeoR and bsCggR in complex with DNA duplexes representing the minimal operator sequence at resolutions of 2.3 and 2.1 Å, respectively. While bsDeoR contains a homeodomain-like HTH-type domain, bsCggR contains a winged helix-turn-helix-type motif. Both proteins form C2-symmetric dimers that recognize two consecutive major grooves, and the protein-DNA interactions have been analyzed in detail. The crystal structures were used to model the interactions of the proteins with the full DNA operators, and a common mode of DNA recognition is proposed that is most likely to be shared by other members of the SorC/DeoR family. PubMed: 34726169DOI: 10.1107/S2059798321009633 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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