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4ON0

Crystal Structure of NolR from Sinorhizobium fredii in complex with oligo AA DNA

4ON0 の概要
エントリーDOI10.2210/pdb4on0/pdb
関連するPDBエントリー4OMY 4OMZ
分子名称NolR, DNA (5 -D(*TP*AP*TP*TP*AP*GP*AP*GP*AP*AP*CP*CP*CP*TP*GP*AP*TP*GP*TP*TP*AP*A)-3 ), DNA (5 -D(*TP*AP*AP*TP*CP*TP*CP*TP*TP*GP*GP*GP*AP*CP*TP*AP*CP*AP*AP*TP*TP*A)-3 ) (3 entities in total)
機能のキーワードhelix-turn-helix, transcription regulator, transcription-dna complex, transcription/dna
由来する生物種Sinorhizobium fredii
詳細
タンパク質・核酸の鎖数8
化学式量合計77982.26
構造登録者
Lee, S.G.,Krishnan, H.B.,Jez, J.M. (登録日: 2014-01-28, 公開日: 2014-04-16, 最終更新日: 2023-09-20)
主引用文献Lee, S.G.,Krishnan, H.B.,Jez, J.M.
Structural basis for regulation of rhizobial nodulation and symbiosis gene expression by the regulatory protein NolR.
Proc.Natl.Acad.Sci.USA, 111:6509-6514, 2014
Cited by
PubMed Abstract: The symbiosis between rhizobial microbes and host plants involves the coordinated expression of multiple genes, which leads to nodule formation and nitrogen fixation. As part of the transcriptional machinery for nodulation and symbiosis across a range of Rhizobium, NolR serves as a global regulatory protein. Here, we present the X-ray crystal structures of NolR in the unliganded form and complexed with two different 22-base pair (bp) double-stranded operator sequences (oligos AT and AA). Structural and biochemical analysis of NolR reveals protein-DNA interactions with an asymmetric operator site and defines a mechanism for conformational switching of a key residue (Gln56) to accommodate variation in target DNA sequences from diverse rhizobial genes for nodulation and symbiosis. This conformational switching alters the energetic contributions to DNA binding without changes in affinity for the target sequence. Two possible models for the role of NolR in the regulation of different nodulation and symbiosis genes are proposed. To our knowledge, these studies provide the first structural insight on the regulation of genes involved in the agriculturally and ecologically important symbiosis of microbes and plants that leads to nodule formation and nitrogen fixation.
PubMed: 24733893
DOI: 10.1073/pnas.1402243111
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3 Å)
構造検証レポート
Validation report summary of 4on0
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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