The C-terminal domain of the transcriptional regulator BldD from Streptomyces coelicolor A3(2) constitutes a novel fold of winged-helix domains

Authors

  • Jeong-Mok Kim,

    1. Laboratory of Biophysics, School of Biological Sciences, and Institute of Microbiology, Seoul National University, Seoul, Republic of Korea
    Search for more papers by this author
  • Hyung-Sik Won,

    Corresponding author
    1. Department of Biotechnology, Research Institute for Biomedical and Health Science, and College of Biomedical and Health Science, Konkuk University, Chungju, Chungbuk, Republic of Korea
    • Correspondence to: Sa-Ouk Kang, Laboratory of Biophysics, School of Biological Sciences, and Institute of Microbiology, Seoul National University, Seoul 151-742, Republic of Korea. E-mail: kangsaou@snu.ac.kr or Hyung-Sik Won, Department of Biotechnology, Research Institute for Biomedical and Health Science, and College of Biomedical and Health Science, Konkuk University, Chungju, Chungbuk 380-701, Republic of Korea. E-mail: wonhs@kku.ac.kr

    Search for more papers by this author
  • Sa-Ouk Kang

    Corresponding author
    1. Laboratory of Biophysics, School of Biological Sciences, and Institute of Microbiology, Seoul National University, Seoul, Republic of Korea
    • Correspondence to: Sa-Ouk Kang, Laboratory of Biophysics, School of Biological Sciences, and Institute of Microbiology, Seoul National University, Seoul 151-742, Republic of Korea. E-mail: kangsaou@snu.ac.kr or Hyung-Sik Won, Department of Biotechnology, Research Institute for Biomedical and Health Science, and College of Biomedical and Health Science, Konkuk University, Chungju, Chungbuk 380-701, Republic of Korea. E-mail: wonhs@kku.ac.kr

    Search for more papers by this author

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. Proteins 2014; 82:1093–1098. © 2013 Wiley Periodicals, Inc.

Ancillary