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Mainchain NMR Assignments and secondary structure prediction of the C-terminal domain of BldD, a developmental transcriptional regulator from Streptomyces coelicolor A3(2)

  • Kim, Jeong-Mok (Laboratory of Biophysics, School of Biological Sciences, and Institute of Microbiology, Seoul National University) ;
  • Won, Hyung-Sik (Department of Biotechnology, Konkuk University) ;
  • Kang, Sa-Ouk (Laboratory of Biophysics, School of Biological Sciences, and Institute of Microbiology, Seoul National University)
  • 투고 : 2013.05.13
  • 심사 : 2013.06.10
  • 발행 : 2013.06.20

초록

BldD, a developmental transcription factor from Streptomyces coelicolor, is a homodimeric, DNA-binding protein with 167 amino acids in each subunit. Each monomer consists of two structurally distinct domains, the N-terminal domain (BldD-NTD) responsible for DNA-binding and dimerization and the C-terminal domain (BldD-CTD). In contrast to the BldD-NTD, of which crystal structure has been solved, the BldD-CTD has been characterized neither in structure nor in function. Thus, in terms of structural genomics, structural study of the BldD-CTD has been conducted in solution, and in the present work, mainchain NMR assignments of the recombinant BldD-CTD (residues 80-167 of BldD) could be achieved by a series of heteronuclear multidimensional NMR experiments on a [$^{13}C/^{15}N$]-enriched protein sample. Finally, the secondary structure prediction by CSI and TALOS+ analysis using the assigned chemical shifts data identified a ${\beta}-{\alpha}-{\alpha}-{\beta}-{\alpha}-{\alpha}-{\alpha}$ topology of the domain. The results will provide the most fundamental data for more detailed approach to the atomic structure of the BldD-CTD, which would be essential for entire understanding of the molecular function of BldD.

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