 |
PDBsum entry 4x9d
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
RNA binding protein
|
PDB id
|
|
|
|
4x9d
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Characterization of RNA-Binding properties of the archaeal hfq-Like protein from methanococcus jannaschii.
|
 |
|
Authors
|
 |
A.Nikulin,
A.Mikhailina,
N.Lekontseva,
V.Balobanov,
E.Nikonova,
S.Tishchenko.
|
 |
|
Ref.
|
 |
J Biomol Struct Dyn, 2017,
35,
1615-1628.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
|
|
 |
 |
|
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.
|
 |
|
|
|
|
 |