PDBsum entry 4x9d

RNA binding protein

PDB id: 4x9d

Contents

Protein chains

56 a.a.

58 a.a.

59 a.a.

Ligands

PGE ×2

SO4 ×2

U5P ×6

EDO

PG4 ×2

PEG

Metals

_NA ×5

_CL ×2

Waters ×241

PDB id:

4x9d

Name:

RNA binding protein

Title:

High-resolution structure of hfq from methanococcus jannaschii in complex with ump

Structure:

Uncharacterized protein mj1435. Chain: a, b, c, d, e, f. Engineered: yes

Source:

Methanocaldococcus jannaschii. Organism_taxid: 2190. Gene: mj1435. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.50Å R-factor: 0.176 R-free: 0.203

Authors:

A.D.Nikulin,S.V.Tishchenko,E.Y.Nikonova,V.N.Murina,A.O.Mihailina, N.V.Lekontseva

Key ref:

A.Nikulin et al. (2017). Characterization of RNA-binding properties of the archaeal Hfq-like protein from Methanococcus jannaschii. J Biomol Struct Dyn, 35, 1615-1628. PubMed id: 27187760 DOI: 10.1080/07391102.2016.1189849

Date:

11-Dec-14 Release date: 23-Dec-15

Protein chain

Q58830  (Y1435_METJA) -  Uncharacterized protein MJ1435 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

Seq: 71 a.a.

Struc: 56 a.a.

Protein chains

Q58830  (Y1435_METJA) -  Uncharacterized protein MJ1435 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

Seq: 71 a.a.

Struc: 58 a.a.

Protein chains

Q58830  (Y1435_METJA) -  Uncharacterized protein MJ1435 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

Seq: 71 a.a.

Struc: 59 a.a.

DOI no: 10.1080/07391102.2016.1189849

J Biomol Struct Dyn 35:1615-1628 (2017)

PubMed id: 27187760

Characterization of RNA-binding properties of the archaeal Hfq-like protein from Methanococcus jannaschii.

A.Nikulin, A.Mikhailina, N.Lekontseva, V.Balobanov, E.Nikonova, S.Tishchenko.

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.