7B1V

DtxR-like iron-dependent regulator IdeR complexed with cobalt

7B1V の概要

• エントリーDOI: 10.2210/pdb7b1v/pdb
• 分子名称: DtxR family iron (Metal) dependent repressor, COBALT (II) ION (3 entities in total)
• 機能のキーワード: transcription, transcription regulation, repressor, regulator, transcription regulator, metal sensor, ider, iron-dependent regulator, dtxr, helix-turn-helix, metal ion, metal-binding protein, dna binding
• 由来する生物種: Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51588.46

構造登録者

Maurer, D.,Marcos-Torres, F.J.,Griese, J.J. (登録日: 2020-11-25, 公開日: 2021-03-03, 最終更新日: 2024-11-13)

主引用文献

Marcos-Torres, F.J.,Maurer, D.,Juniar, L.,Griese, J.J.
The bacterial iron sensor IdeR recognizes its DNA targets by indirect readout.
Nucleic Acids Res., 49:10120-10135, 2021

PubMed Abstract: The iron-dependent regulator IdeR is the main transcriptional regulator controlling iron homeostasis genes in Actinobacteria, including species from the Corynebacterium, Mycobacterium and Streptomyces genera, as well as the erythromycin-producing bacterium Saccharopolyspora erythraea. Despite being a well-studied transcription factor since the identification of the Diphtheria toxin repressor DtxR three decades ago, the details of how IdeR proteins recognize their highly conserved 19-bp DNA target remain to be elucidated. IdeR makes few direct contacts with DNA bases in its target sequence, and we show here that these contacts are not required for target recognition. The results of our structural and mutational studies support a model wherein IdeR mainly uses an indirect readout mechanism, identifying its targets via the sequence-dependent DNA backbone structure rather than through specific contacts with the DNA bases. Furthermore, we show that IdeR efficiently recognizes a shorter palindromic sequence corresponding to a half binding site as compared to the full 19-bp target previously reported, expanding the number of potential target genes controlled by IdeR proteins.

PubMed: 34417623
DOI: 10.1093/nar/gkab711

実験手法

X-RAY DIFFRACTION (2.04 Å)