title: The C-terminal domain of the transcriptional regulator BldD from Streptomyces coelicolor A3(2) constitutes a novel fold of winged-helix domains.
abstract: BldD regulates transcription of key developmental genes in Streptomyces coelicolor. While the N-terminal domain is responsible for both dimerization and DNA binding, the structural and functional roles of the C-terminal domain (CTD) remain largely unexplored. Here, the solution structure of the BldD-CTD shows a novel winged-helix domain fold not compatible with DNA binding, due to the negatively charged surface and presence of an additional helix. Meanwhile, a small elongated groove with conserved hydrophobic patches surrounded by charged residues suggests that the BldD-CTD could be involved in protein-protein interactions that provide transcriptional regulation.
authors.affiliation: Laboratory of Biophysics, School of Biological Sciences, and Institute of Microbiology, Seoul National University, Seoul, 151-742, Republic of Korea.
authors.forename: Jeong-Mok
authors.initials: JM
authors.lastname: Kim
authors.forename: Hyung-Sik
authors.initials: HS
authors.lastname: Won
authors.forename: Sa-Ouk
authors.initials: SO
authors.lastname: Kang
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D017124:Conserved Sequence; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D054730:Protein Interaction Domains and Motifs; D017433:Protein Structure, Secondary; D048372:Streptomyces coelicolor; D051540:Winged-Helix Transcription Factors / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; C111307:BldB protein, Streptomyces coelicolor; D051540:Winged-Helix Transcription Factors
keywords: DNA binding; NMR; bld mutant; solution structure; winged helix-turn-helix