2y7k | pdb_00002y7k

DntR Inducer Binding Domain in Complex with Salicylate. Monoclinic crystal form

spinqualitylabelsall models 2y7k, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2y7k is a 4 chain structure with sequence from Burkholderia sp. DNT. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: SAL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q7WT50_9BURK Publication Abstract from PubMed Activation of LysR-type transcription factors (LTTRs) is thought to result from conformational changes that occur when inducer molecules bind to their Inducer Binding Domains (IBDs). However, the exact nature of these changes remains to be fully elucidated. We present the crystal structures of two truncated constructs of the LTTR DntR in their apo- forms and in complex with its natural inducer molecule, salicylate. These provide a fuller picture of the conformational changes that can occur in LTTR IBDs and offer insights that may be relevant when considering the mechanism of activation of LTTRs. Two of the crystal structures show that DntR IBDs can bind up to two inducer molecules. The full extent of conformational changes observed is achieved only when inducer molecules are bound in both binding sites identified. Point mutations disrupting the putative secondary binding site produce DntR variants with a reduced response to salicylate in a whole cell system, suggesting that this site is functionally relevant. Crystal structures of DntR inducer binding domains in complex with salicylate offer insights into the activation of LysR-type transcriptional regulators.,Devesse L, Smirnova I, Lonneborg R, Kapp U, Brzezinski P, Leonard GA, Dian C Mol Microbiol. 2011 Jul;81(2):354-367. doi:, 10.1111/j.1365-2958.2011.07673.x. Epub 2011 Jun 22. PMID:21692874 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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