1WPV

Crystal Structure of Activated Binary complex of HutP, an RNA binding anti-termination protein

1WPV の概要

• エントリーDOI: 10.2210/pdb1wpv/pdb
• 関連するPDBエントリー: 1VEA 1WMQ 1WPS 1WPT 1WPU
• 分子名称: Hut operon positive regulatory protein, MAGNESIUM ION, HISTIDINE, ... (4 entities in total)
• 機能のキーワード: hutp, rna binding, antitermination, transcription regulation, l-histidine, conformational change, allosteric activation, rna binding protein
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 48845.47

構造登録者

Kumarevel, T.S.,Mizuno, H.,Kumar, P.K.R. (登録日: 2004-09-14, 公開日: 2005-03-15, 最終更新日: 2023-10-25)

主引用文献

Kumarevel, T.,Mizuno, H.,Kumar, P.K.
Structural basis of HutP-mediated anti-termination and roles of the Mg2+ ion and L-histidine ligand.
Nature, 434:183-191, 2005

PubMed Abstract: HutP regulates the expression of the hut structural genes of Bacillus subtilis by an anti-termination mechanism and requires two components, Mg2+ ions and L-histidine. HutP recognizes three UAG triplet units, separated by four non-conserved nucleotides on the terminator region. Here we report the 1.60-A resolution crystal structure of the quaternary complex (HutP-L-histidine-Mg2+-21-base single-stranded RNA). In the complex, the RNA adopts a novel triangular fold on the hexameric surface of HutP, without any base-pairing, and binds to the protein mostly by specific protein-base interactions. The structure explains how the HutP and RNA interactions are regulated critically by the l-histidine and Mg2+ ion through the structural rearrangement. To gain insights into these structural rearrangements, we solved two additional crystal structures (uncomplexed HutP and HutP-L-histidine-Mg2+) that revealed the intermediate structures of HutP (before forming an active structure) and the importance of the Mg2+ ion interactions in the complexes.

PubMed: 15758992
DOI: 10.1038/nature03355

実験手法

X-RAY DIFFRACTION (1.7 Å)