4PNO

Escherichia coli Hfq-RNA complex at 0.97 A Resolution

4PNO の概要

• エントリーDOI: 10.2210/pdb4pno/pdb
• 分子名称: RNA-binding protein Hfq, URIDINE-5'-MONOPHOSPHATE (3 entities in total)
• 機能のキーワード: rna chaperone hfq rna lsm, rna binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8453.62

構造登録者

Schulz, E.C.,Barabas, O. (登録日: 2014-05-24, 公開日: 2014-11-19, 最終更新日: 2023-09-27)

主引用文献

Schulz, E.C.,Barabas, O.
Structure of an Escherichia coli Hfq:RNA complex at 0.97 angstrom resolution.
Acta Crystallogr.,Sect.F, 70:1492-1497, 2014

PubMed Abstract: In bacteria, small RNAs (sRNAs) silence or activate target genes through base pairing with the mRNA, thereby modulating its translation. A central player in this process is the RNA chaperone Hfq, which facilitates the annealing of sRNAs with their target mRNAs. Hfq has two RNA-binding surfaces that recognize A-rich and U-rich sequences, and is believed to bind an sRNA-mRNA pair simultaneously. However, how Hfq promotes annealing remains unclear. Here, the crystal structure of Escherichia coli Hfq is presented in complex with U6-RNA bound to its proximal binding site at 0.97 Å resolution, revealing the Hfq-RNA interaction in exceptional detail.

PubMed: 25372815
DOI: 10.1107/S2053230X14020044

実験手法

X-RAY DIFFRACTION (0.97 Å)