PDBsum entry 2jgn

Hydrolase

PDB id: 2jgn

Contents

Protein chains

151 a.a. *

161 a.a. *

158 a.a. *

Waters ×193

* Residue conservation analysis

PDB id:

2jgn

Name:

Hydrolase

Title:

Ddx3 helicase domain

Structure:

Atp-dependent RNA helicase ddx3x. Chain: a, b, c. Fragment: helicase domain, residues 408-579. Synonym: dbx, ddx3. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.91Å R-factor: 0.201 R-free: 0.255

Authors:

B.Rodamilans,G.Montoya

Key ref:

B.Rodamilans and G.Montoya (2007). Expression, purification, crystallization and preliminary X-ray diffraction analysis of the DDX3 RNA helicase domain. Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 283-286. PubMed id: 17401195

Date:

13-Feb-07 Release date: 13-May-08

Protein chain

O00571  (DDX3X_HUMAN) -  ATP-dependent RNA helicase DDX3X from Homo sapiens

Seq: 662 a.a.

Struc: 151 a.a.

Protein chain

O00571  (DDX3X_HUMAN) -  ATP-dependent RNA helicase DDX3X from Homo sapiens

Seq: 662 a.a.

Struc: 161 a.a.

Protein chain

O00571  (DDX3X_HUMAN) -  ATP-dependent RNA helicase DDX3X from Homo sapiens

Seq: 662 a.a.

Struc: 158 a.a.

Enzyme reactions

• Enzyme class: Chains A, B, C: E.C.3.6.4.13 - Rna helicase.
• Reaction: ATP + H2O = ADP + phosphate + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Acta Crystallogr Sect F Struct Biol Cryst Commun 63:283-286 (2007)

PubMed id: 17401195

Expression, purification, crystallization and preliminary X-ray diffraction analysis of the DDX3 RNA helicase domain.

B.Rodamilans, G.Montoya.

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).