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-Mok; Won, Hyung-Sik; Kang, 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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Collections - 서울 자연과학대학 > 서울 생명과학과 > 1. Journal Articles
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