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

Authors
Kim, Jeong-MokWon, Hyung-SikKang, Sa-Ouk
Issue Date
Jun-2014
Publisher
WILEY-BLACKWELL
Keywords
bld mutant; DNA binding; NMR; solution structure; winged helix-turn-helix
Citation
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, v.82, no.6, pp.1093 - 1098
Indexed
SCIE
SCOPUS
Journal Title
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume
82
Number
6
Start Page
1093
End Page
1098
URI
https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/25856
DOI
10.1002/prot.24481
ISSN
0887-3585
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. (c) 2013 Wiley Periodicals, Inc.
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