6O19
Crystal Structure of Pho7 complex with pho1 promoter site 2
Summary for 6O19
Entry DOI | 10.2210/pdb6o19/pdb |
Related | 6E33 |
Descriptor | Transcription factor Pho7, DNA (5'-D(*TP*TP*AP*TP*TP*CP*GP*GP*AP*AP*AP*TP*TP*AP*AP*AP*AP*AP*CP*A)-3'), DNA (5'-D(*GP*TP*TP*TP*TP*TP*AP*AP*TP*TP*TP*CP*CP*GP*AP*AP*TP*AP*AP*T)-3'), ... (5 entities in total) |
Functional Keywords | zn2cys6, zinc binuclear cluster transcription factor, transcription factor-dna complex, pho7, transcription, transcription-dna complex, transcription/dna |
Biological source | Schizosaccharomyces pombe (Fission yeast) More |
Total number of polymer chains | 3 |
Total formula weight | 19156.01 |
Authors | Garg, A.,Goldgur, Y.,Shuman, S. (deposition date: 2019-02-18, release date: 2019-04-24, Last modification date: 2023-10-11) |
Primary citation | Garg, A.,Goldgur, Y.,Sanchez, A.M.,Schwer, B.,Shuman, S. Structure of Fission Yeast Transcription Factor Pho7 Bound topho1Promoter DNA and Effect of Pho7 Mutations on DNA Binding and Phosphate Homeostasis. Mol.Cell.Biol., 39:-, 2019 Cited by PubMed Abstract: Pho7 is the fission yeast ZnCys transcriptional factor that drives a response to phosphate starvation in which phosphate acquisition genes are upregulated. Here we report a crystal structure at 1.6-Å resolution of the Pho7 DNA-binding domain (DBD) bound at its target site 2 in the promoter (5'-TCGGAAATTAAAAA). Comparison to the previously reported structure of Pho7 DBD in complex with its binding site in the promoter (5'-TCGGACATTCAAAT) reveals shared determinants of target site specificity as well as variations in the protein-DNA interface that accommodate different promoter DNA sequences. Mutagenesis of Pho7 amino acids at the DNA interface identified nucleobase contacts at the periphery of the footprint that are essential for the induction of expression in response to phosphate starvation and for Pho7 binding to site 1 in the promoter. PubMed: 31010807DOI: 10.1128/MCB.00132-19 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.596 Å) |
Structure validation
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