5H1A

Crystal structure of an IclR homolog from Microbacterium sp. strain HM58-2

5H1A の概要

• エントリーDOI: 10.2210/pdb5h1a/pdb
• 分子名称: IclR transcription factor homolog, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: dna-binding, transcription regulator
• 由来する生物種: Microbacterium sp.
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 117389.87

構造登録者

Akiyama, T.,Yamada, Y.,Takaya, N.,Ito, S.,Sasaki, Y.,Yajima, S. (登録日: 2016-10-08, 公開日: 2017-01-18, 最終更新日: 2024-03-20)

主引用文献

Akiyama, T.,Yamada, Y.,Takaya, N.,Ito, S.,Sasaki, Y.,Yajima, S.
Crystal structure of an IclR homologue from Microbacterium sp. strain HM58-2.
Acta Crystallogr F Struct Biol Commun, 73:16-23, 2017

PubMed Abstract: The bacterial transcription factor IclR (isocitrate lyase regulator) is a member of a one-component signal transduction system, which shares the common motif of a helix-turn-helix (HTH)-type DNA-binding domain (DBD) connected to a substrate-binding domain (SBD). Here, the crystal structure of an IclR homologue (Mi-IclR) from Microbacterium sp. strain HM58-2, which catabolizes acylhydrazide as the sole carbon source, is reported. Mi-IclR is expected to regulate an operon responsible for acylhydrazide degradation as an initial step. Native single-wavelength anomalous diffraction (SAD) experiments were performed in combination with molecular replacement. CRANK2 from the CCP4 suite successfully phased and modelled the complete structure of a homotetramer composed of 1000 residues in an asymmetric unit, and the model was refined to 2.1 Å resolution. The overall structure of Mi-IclR shared the same domain combination as other known IclR structures, but the relative geometry between the DBD and SBD differs. Accordingly, the geometry of the Mi-IclR tetramer was unique: the putative substrate-binding site in each subunit is accessible from the outside of the tetramer, as opposed to buried inside as in the previously known IclR structures. These differences in the domain geometry may contribute to the transcriptional regulation of IclRs.

PubMed: 28045389
DOI: 10.1107/S2053230X16019208

実験手法

X-RAY DIFFRACTION (2.1 Å)