6E33

Crystal Structure of Pho7-DNA complex

6E33 の概要

• エントリーDOI: 10.2210/pdb6e33/pdb
• 分子名称: Uncharacterized transcriptional regulatory protein C27B12.11c, DNA (5'-D(*TP*CP*CP*TP*TP*CP*GP*GP*AP*CP*AP*TP*TP*CP*AP*AP*AP*TP*CP*A)-3'), DNA (5'-D(*GP*AP*TP*TP*TP*GP*AP*AP*TP*GP*TP*CP*CP*GP*AP*AP*GP*GP*AP*T)-3'), ... (5 entities in total)
• 機能のキーワード: zn2cys6, zinc binuclear cluster transcription factor, transcription factor-dna complex, pho7, transcription
• 由来する生物種: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 19402.29

構造登録者

Garg, A.,Goldgur, Y.,Shuman, S. (登録日: 2018-07-13, 公開日: 2018-10-24, 最終更新日: 2024-03-13)

主引用文献

Garg, A.,Goldgur, Y.,Schwer, B.,Shuman, S.
Distinctive structural basis for DNA recognition by the fission yeast Zn2Cys6 transcription factor Pho7 and its role in phosphate homeostasis.
Nucleic Acids Res., 46:11262-11273, 2018

PubMed Abstract: Pho7, a member of the Zn2Cys6 family of fungal transcription factors, is the key transcriptional activator underlying fission yeast phosphate homeostasis, a physiological response to phosphate starvation in which the pho1, pho84 and tgp1 genes are upregulated. Here, we delineated a minimized 61-amino-acid Pho7 DNA-binding domain (DBD) and determined the 1.7 Å crystal structure of the DBD at its target site in the tgp1 promoter. Two distinctive features of the Pho7 DBD are: it binds DNA as a monomer, unlike most other fungal zinc-cluster factors that bind as homodimers; and it makes extensive interactions with its asymmetric target sequence over a 14-bp footprint that entails hydrogen bonding to 13 individual bases within, and remote from, the CGG triplet typically recognized by other Zn2Cys6 DBDs. Base pair substitutions at Pho7 sites in the tgp1 and pho1 promoters highlight the importance of the 5'-CGG triplet for Pho7 binding in vitro and Pho7-dependent gene expression in vivo. We identify several DBD amino acids at which alanine substitution effaced or attenuated the pho1 phosphate starvation response and concordantly reduced Pho7 binding to a pho1 promoter site.

PubMed: 30212894
DOI: 10.1093/nar/gky827

実験手法

X-RAY DIFFRACTION (1.705 Å)