2WV0
Crystal structure of the GntR-HutC family member YvoA from Bacillus subtilis
Summary for 2WV0
| Entry DOI | 10.2210/pdb2wv0/pdb |
| Descriptor | HTH-TYPE TRANSCRIPTIONAL REPRESSOR YVOA, SULFATE ION (3 entities in total) |
| Functional Keywords | repressor, dna-binding, transcription, transcription regulation, transcriptional regulator, gntr/hutc family, chorismate lyase fold |
| Biological source | BACILLUS SUBTILIS |
| Total number of polymer chains | 10 |
| Total formula weight | 276854.70 |
| Authors | Resch, M.,Schiltz, E.,Titgemeyer, F.,Muller, Y.A. (deposition date: 2009-10-12, release date: 2010-01-12, Last modification date: 2024-05-08) |
| Primary citation | Resch, M.,Schiltz, E.,Titgemeyer, F.,Muller, Y.A. Insight Into the Induction Mechanism of the Gntr/Hutc Bacterial Transcription Regulator Yvoa Nucleic Acids Res., 38:2485-, 2010 Cited by PubMed Abstract: 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. PubMed: 20047956DOI: 10.1093/NAR/GKP1191 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
Download full validation report
