4X9C

1.4A crystal structure of Hfq from Methanococcus jannaschii

Summary for 4X9C

• Entry DOI: 10.2210/pdb4x9c/pdb
• Related: 2QTX
• Descriptor: Uncharacterized protein MJ1435, DI(HYDROXYETHYL)ETHER, TRIETHYLENE GLYCOL, ... (9 entities in total)
• Functional Keywords: hfq, lsm proteins, archaea, rna binding protein
• Biological source: Methanocaldococcus jannaschii
• Total number of polymer chains: 6
• Total formula weight: 51652.85

Authors

Nikulin, A.D.,Tishchenko, S.V.,Nikonova, S.V.,Murina, V.N.,Mihailina, A.O.,Lekontseva, N.V. (deposition date: 2014-12-11, release date: 2014-12-24, Last modification date: 2024-01-10)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.4 Å)