7bhy
From Proteopedia
DNA-binding domain of DeoR in complex with the DNA operator
Structural highlights
FunctionDEOR_BACSU Negative regulator of the dra-nupC-pdp operon. DeoR binds cooperatively to the operator DNA, which consists of a palindrome and a direct repeat sequence located 3' to the palindrome. Publication Abstract from PubMedThe 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 A, respectively. While bsDeoRDBD contains a homeodomain-like HTH-type domain, bsCggRDBD 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. Structural insight into DNA recognition by bacterial transcriptional regulators of the SorC/DeoR family.,Soltysova M, Sieglova I, Fabry M, Brynda J, Skerlova J, Rezacova P Acta Crystallogr D Struct Biol. 2021 Nov 1;77(Pt 11):1411-1424. doi:, 10.1107/S2059798321009633. Epub 2021 Oct 20. PMID:34726169[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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