4UX5
Structure of DNA complex of PCG2
Summary for 4UX5
Entry DOI | 10.2210/pdb4ux5/pdb |
Descriptor | TRANSCRIPTION FACTOR MBP1, 5'-D(*CP*AP*AP*TP*GP*AP*CP*GP*CP*GP*TP*AP*AP*GP)-3', 5'-D(*CP*TP*TP*AP*CP*GP*CP*GP*TP*CP*AP*TP*TP*GP)-3', ... (4 entities in total) |
Functional Keywords | transcription, virulence gene, transcription factor |
Biological source | MAGNAPORTHE ORYZAE (RICE BLAST FUNGUS) More |
Total number of polymer chains | 4 |
Total formula weight | 38939.07 |
Authors | |
Primary citation | Liu, J.,Huang, J.,Zhao, Y.,Liu, H.,Wang, D.,Yang, J.,Zhao, W.,Taylor, I.A.,Peng, Y. Structural Basis of DNA Recognition by Pcg2 Reveals a Novel DNA Binding Mode for Winged Helix-Turn-Helix Domains. Nucleic Acids Res., 43:1231-, 2015 Cited by PubMed Abstract: The MBP1 family proteins are the DNA binding subunits of MBF cell-cycle transcription factor complexes and contain an N terminal winged helix-turn-helix (wHTH) DNA binding domain (DBD). Although the DNA binding mechanism of MBP1 from Saccharomyces cerevisiae has been extensively studied, the structural framework and the DNA binding mode of other MBP1 family proteins remains to be disclosed. Here, we determined the crystal structure of the DBD of PCG2, the Magnaporthe oryzae orthologue of MBP1, bound to MCB-DNA. The structure revealed that the wing, the 20-loop, helix A and helix B in PCG2-DBD are important elements for DNA binding. Unlike previously characterized wHTH proteins, PCG2-DBD utilizes the wing and helix-B to bind the minor groove and the major groove of the MCB-DNA whilst the 20-loop and helix A interact non-specifically with DNA. Notably, two glutamines Q89 and Q82 within the wing were found to recognize the MCB core CGCG sequence through making hydrogen bond interactions. Further in vitro assays confirmed essential roles of Q89 and Q82 in the DNA binding. These data together indicate that the MBP1 homologue PCG2 employs an unusual mode of binding to target DNA and demonstrate the versatility of wHTH domains. PubMed: 25550425DOI: 10.1093/NAR/GKU1351 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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