2wv0

Crystal structure of the GntR-HutC family member YvoA from Bacillus subtilis

spinqualitylabelsall models 2wv0, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wv0 is a 10 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NAGR_BACSU Main transcriptional repressor of genes involved in N-acetylglucosamine (GlcNAc) transport and utilization (PubMed:21602348, PubMed:20047956, PubMed:24673833). Represses the expression of the nagAB and nagP operons by binding directly within their upstream regions (PubMed:21602348, PubMed:24673833). Binds to the DNA consensus sequence 5'-ATTGGTATAGACAACT-3' (PubMed:21602348). Also acts as a weak repressor of mapB expression (PubMed:16207374). 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 YvoA is a GntR/HutC transcription regulator from Bacillus subtilis implicated in the regulation of genes from the N-acetylglucosamine-degrading pathway. Its 2.4-A crystal structure reveals a homodimeric assembly with each monomer displaying a two-domain fold. The C-terminal domain, which binds the effector N-acetylglucosamine-6-phosphate, adopts a chorismate lyase fold, whereas the N-terminal domain contains a winged helix-turn-helix DNA-binding domain. Isothermal titration calorimetry and site-directed mutagenesis revealed that the effector-binding site in YvoA coincides with the active site of related chorismate lyase from Escherichia coli. The characterization of the DNA- and effector-binding properties of two disulfide-bridged mutants that lock YvoA in two distinct conformational states provides for the first time detailed insight into the allosteric mechanism through which effector binding modulates DNA binding and, thereby regulates transcription in a representative GntR/HutC family member. Central to this allosteric coupling mechanism is a loop-to-helix transition with the dipole of the newly formed helix pointing toward the phosphate of the effector. This transition goes in hand with the emergence of internal symmetry in the effector-binding domain and, in addition, leads to a 122 degrees rotation of the DNA-binding domains that is best described as a jumping-jack-like motion. Insight into the induction mechanism of the GntR/HutC bacterial transcription regulator YvoA.,Resch M, Schiltz E, Titgemeyer F, Muller YA Nucleic Acids Res. 2010 Apr;38(7):2485-97. Epub 2010 Jan 4. PMID:20047956 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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