2jgn

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{{STRUCTURE_2jgn| PDB=2jgn | SCENE= }}
{{STRUCTURE_2jgn| PDB=2jgn | SCENE= }}
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'''DDX3 HELICASE DOMAIN'''
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===DDX3 HELICASE DOMAIN===
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==Overview==
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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).
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==About this Structure==
==About this Structure==
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[[Category: Phosphorylation]]
[[Category: Phosphorylation]]
[[Category: Rna-binding]]
[[Category: Rna-binding]]
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Revision as of 17:39, 28 July 2008

Image:2jgn.png

Template:STRUCTURE 2jgn

DDX3 HELICASE DOMAIN

Template:ABSTRACT PUBMED 17401195

About this Structure

2JGN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Expression, purification, crystallization and preliminary X-ray diffraction analysis of the DDX3 RNA helicase domain., Rodamilans B, Montoya G, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt, 4):283-6. Epub 2007 Mar 12. PMID:17401195

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