5DY9

Y68T Hfq from Methanococcus jannaschii in complex with AMP

5DY9 の概要

• エントリーDOI: 10.2210/pdb5dy9/pdb
• 関連するPDBエントリー: 2QTX 4X9C 4X9D
• 分子名称: Hfq-like protein, ADENOSINE MONOPHOSPHATE, GLYCEROL, ... (9 entities in total)
• 機能のキーワード: hfq, lsm protein, ribonucleotide-protein complex, rna binding protein
• 由来する生物種: Methanocaldococcus jannaschii DSM 2661
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 101582.63

構造登録者

Nikulin, A.D.,Mikhailina, A.O.,Lekontseva, N.V.,Balobanov, V.A.,Nikonova, E.Y.,Tishchenko, S.V. (登録日: 2015-09-24, 公開日: 2016-09-28, 最終更新日: 2024-05-08)

主引用文献

Nikulin, A.,Mikhailina, A.,Lekontseva, N.,Balobanov, V.,Nikonova, E.,Tishchenko, S.
Characterization of RNA-binding properties of the archaeal Hfq-like protein from Methanococcus jannaschii.
J. Biomol. Struct. Dyn., 35:1615-1628, 2017

PubMed Abstract: The Sm and Sm-like proteins are widely distributed among bacteria, archaea and eukarya. They participate in many processes related to RNA-processing and regulation of gene expression. While the function of the bacterial Lsm protein Hfq and eukaryotic Sm/Lsm proteins is rather well studied, the role of Lsm proteins in Archaea is investigated poorly. In this work, the RNA-binding ability of an archaeal Hfq-like protein from Methanococcus jannaschii has been studied by X-ray crystallography, anisotropy fluorescence and surface plasmon resonance. It has been found that MjaHfq preserves the proximal RNA-binding site that usually recognizes uridine-rich sequences. Distal adenine-binding and lateral RNA-binding sites show considerable structural changes as compared to bacterial Hfq. MjaHfq did not bind mononucleotides at these sites and would not recognize single-stranded RNA as its bacterial homologues. Nevertheless, MjaHfq possesses affinity to poly(A) RNA that seems to bind at the unstructured positive-charged N-terminal tail of the protein.

PubMed: 27187760
DOI: 10.1080/07391102.2016.1189849

実験手法

X-RAY DIFFRACTION (1.6 Å)