5gp9

Structural analysis of fatty acid degradation regulator FadR from Bacillus halodurans

spinqualitylabelsall models 5gp9, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5gp9 is a 2 chain structure with sequence from Alkalihalobacillus halodurans C-125. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.755Å Ligands: GOL, MG, PLM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9K8A4_HALH5 Publication Abstract from PubMed FadR is a fatty acyl-CoA dependent transcription factor that regulates genes encoding proteins involved in fatty-acid degradation and synthesis pathways. In this study, the crystal structures of Bacillus halodurans FadR, which belong to the TetR family, have been determined in three different forms: ligand-bound, ligand-free and DNA-bound at resolutions of 1.75, 2.05 and 2.80 A, respectively. Structural and functional data showed that B. halodurans FadR was bound to its operator site without fatty acyl-CoAs. Structural comparisons among the three different forms of B. halodurans FadR revealed that the movement of DNA binding domains toward the operator DNA was blocked upon binding of ligand molecules. These findings suggest that the TetR family FadR negatively regulates the genes involved in fatty acid metabolism by binding cooperatively to the operator DNA as a dimer of dimers. Structural basis of operator sites recognition and effector binding in the TetR family transcription regulator FadR.,Yeo HK, Park YW, Lee JY Nucleic Acids Res. 2017 Apr 20;45(7):4244-4254. doi: 10.1093/nar/gkx009. PMID:28160603 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tetracycline repressor protein 3D structures Transcriptional activator 3D structures

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