3HSB

Crystal structure of YmaH (Hfq) from Bacillus subtilis in complex with an RNA aptamer

3HSB の概要

• エントリーDOI: 10.2210/pdb3hsb/pdb
• 分子名称: Protein hfq, RNA (5'-R(*AP*GP*AP*GP*AP*GP*A)-3') (3 entities in total)
• 機能のキーワード: sm-like motif, protein-rna complex, rna-binding, stress response, rna binding protein-rna complex, rna binding protein/rna
• 由来する生物種: Bacillus subtilis; 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 55912.77

構造登録者

Baba, S.,Someya, T.,Kumasaka, T.,Kawai, G.,Nakamura, K. (登録日: 2009-06-10, 公開日: 2010-06-23, 最終更新日: 2023-11-01)

主引用文献

Someya, T.,Baba, S.,Fujimoto, M.,Kawai, G.,Kumasaka, T.,Nakamura, K.
Crystal structure of Hfq from Bacillus subtilis in complex with SELEX-derived RNA aptamer: insight into RNA-binding properties of bacterial Hfq
Nucleic Acids Res., 40:1856-1867, 2012

PubMed Abstract: Bacterial Hfq is a protein that plays an important role in the regulation of genes in cooperation with sRNAs. Escherichia coli Hfq (EcHfq) has two or more sites that bind RNA(s) including U-rich and/or the poly(A) tail of mRNA. However, functional and structural information about Bacillus subtilis Hfq (BsHfq) including the RNA sequences that specifically bind to it remain unknown. Here, we describe RNA aptamers including fragment (AG)(3)A that are recognized by BsHfq and crystal structures of the BsHfq-(AG)(3)A complex at 2.2 Å resolution. Mutational and structural studies revealed that the RNA fragment binds to the distal site, one of the two binding sites on Hfq, and identified amino acid residues that are critical for sequence-specific interactions between BsHfq and (AG)(3)A. In particular, R32 appears to interact with G bases in (AG)(3)A. Poly(A) also binds to the distal site of EcHfq, but the overall RNA structure and protein-RNA interaction patterns engaged in the R32 residues of BsHfq-(AG)(3)A differ from those of EcHfq-poly(A). These findings provide novel insight into how the Hfq homologue recognizes RNA.

PubMed: 22053080
DOI: 10.1093/nar/gkr892

実験手法

X-RAY DIFFRACTION (2.2 Å)