4OMZ
Crystal Structure of NolR from Sinorhizobium fredii
4OMZ の概要
| エントリーDOI | 10.2210/pdb4omz/pdb |
| 分子名称 | NolR, PHOSPHATE ION (3 entities in total) |
| 機能のキーワード | helix-turn-helix, transcription regulator, transcription |
| 由来する生物種 | Sinorhizobium fredii |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 103294.95 |
| 構造登録者 | |
| 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: 24733893DOI: 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 (2.64 Å) |
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