4H4L

Crystal Structure of ternary complex of HutP(HutP-L-His-Zn)

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4H4L の概要

• エントリーDOI: 10.2210/pdb4h4l/pdb
• 分子名称: Hut operon positive regulatory protein, HISTIDINE, ZINC ION, ... (4 entities in total)
• 機能のキーワード: hutp, anti-termination, histidine metabolism, transcription, transcription regulation, rna binding protein
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 197449.49

構造登録者

Dhakshnamoorthy, B.,Misono, T.S.,Mizuno, H.,Kumar, P.K.R. (登録日: 2012-09-17, 公開日: 2013-09-04, 最終更新日: 2023-11-08)

主引用文献

Dhakshnamoorthy, B.,Mizuno, H.,Kumar, P.K.R.
Alternative binding modes of l-histidine guided by metal ions for the activation of the antiterminator protein HutP of Bacillus subtilis.
J.Struct.Biol., 183:512-518, 2013

PubMed Abstract: Anti-terminator proteins control gene expression by recognizing control signals within cognate transcripts and then preventing transcription termination. HutP is such a regulatory protein that regulates the expression of the histidine utilization (hut) operon in Bacillus subtilis by binding to cis-acting regulatory sequences in hut mRNAs. During the anti-termination process, l-histidine and a divalent ion are required for hutP to bind to the specific sequence within the hut mRNA. Our previous crystal structure of the HutP-l-histidine-Mg(2+)-RNA ternary complex demonstrated that the l-histidine ligand and Mg(2+) bind together such that the backbone nitrogen and carboxyl oxygen of l-histidine coordinate with Mg(2+). In addition to the Mg(2+), other divalent ions are also known to efficiently support the l-histidine-dependent anti-termination of the hut operon, and the best divalent ion is Zn(2+). In this study, we determined the crystal structure of the HutP-l-histidine-Zn(2+) complex and found that the orientation of l-histidine coordinated to Zn(2+) is reversed relative to that of l-histidine coordinated to Mg(2+), i.e., the imidazole side chain nitrogen of l-histidine coordinates to Zn(2+). This alternative binding mode of the l-histidine ligand to a divalent ion provides further insight into the mechanisms responsible for the activation of RNA binding during the hut anti-termination process.

PubMed: 23748184
DOI: 10.1016/j.jsb.2013.05.019

実験手法

X-RAY DIFFRACTION (2.5 Å)