期刊
EMBO JOURNAL
卷 20, 期 8, 页码 2041-2050出版社
OXFORD UNIV PRESS
DOI: 10.1093/emboj/20.8.2041
关键词
acyl-CoA; fatty acid; protein structure; regulation; transcription
资金
- Wellcome Trust Funding Source: Medline
FadR is an acyl-Coh-responsive transcription factor, regulating fatty acid biosynthetic and degradation genes in Escherichia coli, The ape-protein binds DNA as a homodimer, an interaction that is disrupted by binding of acyl-CoA, The recently described structure of apo-FadR shows a DNA binding domain coupled to an acyl-CoA binding domain with a novel fold, but does not explain how binding of the acyl-CoA effector molecule > 30 Angstrom away from the DNA binding site affects transcriptional regulation. Here, we describe the structures of the FadR-operator and FadR-myristoyl-CoA binary complexes. The FadR-DNA complex reveals a novel winged helix-turn-helix protein-DNA interaction, involving sequence-specific contacts from the wing to the minor groove. Binding of acyl-CoA results in dramatic conformational changes throughout the protein, with backbone shifts up to 4.5 Angstrom, The net effect is a rearrangement of the DNA binding domains in the dimer, resulting in a change of 7.2 Angstrom in separation of the DNA recognition helices and the loss of DNA binding, revealing the molecular basis of acyl-CoA-responsive regulation.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据