4pxi

Elucidation of the Structural and Functional Mechanism of Action of the TetR Family Protein, CprB from S. coelicolor A3(2)

spinqualitylabelsall models 4pxi, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pxi is a 6 chain structure with sequence from Streptomyces coelicolor and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O66122_STRCH Publication Abstract from PubMed Antibiotic production and resistance pathways in Streptomyces are dictated by the interplay of transcriptional regulatory proteins that trigger downstream responses via binding to small diffusible molecules. To decipher the mode of DNA binding and the associated allosteric mechanism in the sub-class of transcription factors that are induced by gamma-butyrolactones, we present the crystal structure of CprB in complex with the consensus DNA element to a resolution of 3.25 A. Binding of the DNA results in the restructuring of the dimeric interface of CprB, inducing a pendulum-like motion of the helix-turn-helix motif that inserts into the major groove. The crystal structure revealed that, CprB is bound to DNA as a dimer of dimers with the mode of binding being analogous to the broad spectrum multidrug transporter protein QacR from the antibiotic resistant strain Staphylococcus aureus. It was demonstrated that the CprB displays a cooperative mode of DNA binding, following a clamp and click model. Experiments performed on a subset of DNA sequences from Streptomyces coelicolor A3(2) suggest that CprB is most likely a pleiotropic regulator. Apart from serving as an autoregulator, it is potentially a part of a network of proteins that modulates the gamma-butyrolactone synthesis and antibiotic regulation pathways in S. coelicolor A3(2). Structural and functional basis of transcriptional regulation by TetR family protein CprB from S. coelicolor A3(2).,Bhukya H, Bhujbalrao R, Bitra A, Anand R Nucleic Acids Res. 2014 Sep;42(15):10122-33. doi: 10.1093/nar/gku587. Epub 2014, Aug 4. PMID:25092919 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tetracycline repressor protein 3D structures

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