3fxu

Crystal structure of TsaR in complex with its effector p-toluenesulfonate

spinqualitylabelsall models 3fxu, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3fxu is a 2 chain structure with sequence from Comamonas testosteroni. 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: CL, FMT, GOL, IMD, TSU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TSAR_COMTE Regulates expression of the tsaMBCD1 operon and of tsaT in response to p-toluenesulfonate (TSA). Acts by binding directly to the promoter region. Binding to the tsa promoter depends on TSA concentration. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed LysR-type transcriptional regulators (LTTRs) constitute the largest family of regulators in prokaryotes. The full-length structures of the LTTR TsaR from Comamonas testosteroni T-2 and its complex with the natural inducer para-toluensulfonate have been characterized by X-ray diffraction. Both ligand-free and complexed forms reveal a dramatically different quaternary structure from that of CbnR from Ralstonia eutropha, or a putative LysR-type regulator from Pseudomonas aeruginosa, the only other determined full-length structures of tetrameric LTTRs. Although all three show a head-to-head tetrameric ring, TsaR displays an open conformation, whereas CbnR and PA01-PR present additional contacts in opposing C-terminal domains that close the ring. Such large differences may be due to a broader structural versatility than previously assumed or either, reflect the intrinsic flexibility of tetrameric LTTRs. On the grounds of the sliding dimer hypothesis of LTTR activation, we propose a structural model in which the closed structures could reflect the conformation of a ligand-free LTTR, whereas inducer binding would bring about local changes to disrupt the interface linking the two compact C-terminal domains. This could lead to a TsaR-like, open structure, where the pairs of recognition helices are closer to each other by more than 10 A. Structural studies on the full-length LysR-type regulator TsaR from Comamonas testosteroni T-2 reveal a novel open conformation of the tetrameric LTTR fold.,Monferrer D, Tralau T, Kertesz MA, Dix I, Sola M, Uson I Mol Microbiol. 2010 Mar;75(5):1199-214. Epub 2010 Jan 5. PMID:20059681 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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