7VN8
Crystal structure of MBP-fused BIL1/BZR1 (21-90) in complex with double-stranded DNA contaning GTCACGTGAC
7VN8 の概要
エントリーDOI | 10.2210/pdb7vn8/pdb |
関連するBIRD辞書のPRD_ID | PRD_900001 |
分子名称 | Maltodextrin-binding protein,Protein BRASSINAZOLE-RESISTANT 1, DNA (5'-D(*TP*TP*GP*TP*CP*AP*CP*GP*TP*GP*AP*CP*AP*AP*A)-3'), alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (5 entities in total) |
機能のキーワード | transcription factor-dna complex, transcription |
由来する生物種 | Serratia sp. (strain FS14) 詳細 |
タンパク質・核酸の鎖数 | 8 |
化学式量合計 | 214103.32 |
構造登録者 | |
主引用文献 | Nosaki, S.,Mitsuda, N.,Sakamoto, S.,Kusubayashi, K.,Yamagami, A.,Xu, Y.,Bui, T.B.C.,Terada, T.,Miura, K.,Nakano, T.,Tanokura, M.,Miyakawa, T. Brassinosteroid-induced gene repression requires specific and tight promoter binding of BIL1/BZR1 via DNA shape readout. Nat.Plants, 8:1440-1452, 2022 Cited by PubMed Abstract: BRZ-INSENSITIVE-LONG 1 (BIL1)/BRASSINAZOLE-RESISTANT 1 (BZR1) and its homologues are plant-specific transcription factors that convert the signalling of the phytohormones brassinosteroids (BRs) to transcriptional responses, thus controlling various physiological processes in plants. Although BIL1/BZR1 upregulates some BR-responsive genes and downregulates others, the molecular mechanism underlying the dual roles of BIL1/BZR1 is still poorly understood. Here we show that BR-responsive transcriptional repression by BIL1/BZR1 requires the tight binding of BIL1/BZR1 alone to the 10 bp elements of DNA fragments containing the known 6 bp core-binding motifs at the centre. Furthermore, biochemical and structural evidence demonstrates that the selectivity for two nucleobases flanking the core motifs is realized by the DNA shape readout of BIL1/BZR1 without direct recognition of the nucleobases. These results elucidate the molecular and structural basis of transcriptional repression by BIL1/BZR1 and contribute to further understanding of the dual roles of BIL1/BZR1 in BR-responsive gene regulation. PubMed: 36522451DOI: 10.1038/s41477-022-01289-6 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.04 Å) |
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