Solution structure of the GUCT domain from human ATP-dependent RNA helicase
DDX50, DEAD box protein 50

ATP-dependent RNA helicase DDX50 (E.C.3.6.1.-)

Chemical shift reference of 1H was based on the proton of water (4.784ppm at
298K) and then those of 15N and 13C were calculated based on their gyromagnetic
ratios.

Solution structure of the GUCT domain from human RNA helicase II/Gu beta reveals the RRM fold, but implausible RNA interactions.

Solution Structure Of The Guct Domain From Human Atp- Dependent Rna Helicase Ddx50, Dead Box Protein 50

DEAD (Asp-Glu-Ala-Asp) box polypeptide 50 [Homo sapiens]

DEAD (Asp-Glu-Ala-Asp) box polypeptide 50 [synthetic construct]

ATP-dependent RNA helicase DDX50 [Macaca mulatta]

ATP-dependent RNA helicase DDX50 [Homo sapiens]

PREDICTED: ATP-dependent RNA helicase DDX50 isoform X1 [Callithrix jacchus]

PREDICTED: ATP-dependent RNA helicase DDX50 isoform X1 [Pongo abelii]

PREDICTED: ATP-dependent RNA helicase DDX50 isoform X1 [Nomascus leucogenys]

RecName: Full=ATP-dependent RNA helicase DDX50; AltName: Full=DEAD box protein 50; AltName: Full=Gu-beta; AltName: Full=Nucleol

The structure of the GUCT domain (2E29) was determined using the NOE constraints
and the RDC (residual dipolar coupling) constraints.

torsion angle dynamics, restrained molecular dynamics

Protein Research Group, RIKEN Genomic Sciences Center

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax