2JGN

DDX3 helicase domain

Summary for 2JGN

• Entry DOI: 10.2210/pdb2jgn/pdb
• Descriptor: ATP-DEPENDENT RNA HELICASE DDX3X (2 entities in total)
• Functional Keywords: phosphorylation, nucleotide-binding, helicase, hydrolase, rna-binding, atp-binding, dna-binding, nuclear protein, host-virus interaction
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Nucleus speckle: O00571
• Total number of polymer chains: 3
• Total formula weight: 63517.79

Authors

Rodamilans, B.,Montoya, G. (deposition date: 2007-02-13, release date: 2008-05-13, Last modification date: 2023-12-13)

Primary citation

Rodamilans, B.,Montoya, G.
Expression, Purification, Crystallization and Preliminary X-Ray Diffraction Analysis of the Ddx3 RNA Helicase Domain.
Acta Crystallogr.,Sect.F, 63:283-, 2007

PubMed Abstract: DDX3 is a human RNA helicase that is involved in RNA processing and important human diseases. This enzyme belongs to the DEAD-box protein family, the members of which are characterized by the presence of nine conserved motifs including the Asp-Glu-Ala-Asp motif that defines the family. DDX3 has two distinct domains: an ATP-binding domain in the central region of the protein and a helicase domain in the carboxy-terminal region. The helicase domain of DDX3 was cloned and overexpressed in Escherichia coli. Crystallization experiments yielded crystals that were suitable for X-ray diffraction analysis. The final crystallization conditions were a reservoir solution consisting of 2 M ammonium sulfate, 0.1 M imidazole pH 6.4 plus 5 mM spermine tetrahydrochloride and a protein solution containing 10 mM HEPES, 500 mM ammonium sulfate pH 8.0. The crystals of the helicase domain belong to the monoclinic space group P2(1), with unit-cell parameters a = 43.85, b = 60.72, c = 88.39 A, alpha = gamma = 90, beta = 101.02 degrees , and contained three molecules per asymmetric unit. These crystals diffracted to a resolution limit of 2.2 A using synchrotron radiation at the European Synchrotron Radiation Facility (ESRF) and the Swiss Light Source (SLS).

PubMed: 17401195
DOI: 10.1107/S1744309107006434

Experimental method

X-RAY DIFFRACTION (1.91 Å)