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Crystal Structure of Conserved Domains 1 and 2 of the Human DEAD-box Helicase DDX3X in Complex with the Mononucleotide AMP
Södertörn University, School of Life Sciences.
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2007 (English)In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 372, no 1, 150-159 p.Article in journal (Refereed) Published
Abstract [en]

DExD-box helicases are involved in all aspects of cellular RNA metabolism. Conserved domains 1 and 2 contain nine signature motifs that are responsible for nucleotide binding, RNA binding and ATP hydrolysis. The human DEAD-box helicase DDX3X has been associated with several different cellular processes, such as cell-growth control, mRNA transport and translation, and is suggested to be essential for the export of unspliced/partially spliced HIV mRNAs from the nucleus to the cytoplasm. Here, the crystal structure of conserved domains 1 and 2 of DDX3X, including a DDX3-specific insertion that is not generally found in human DExD-box helicases, is presented. The N-terminal domain 1 and the C-terminal domain 2 both display RecA-like folds comprising a central β-sheet flanked by α-helices. Interestingly, the DDX3X-specific insertion forms a helical element that extends a highly positively charged sequence in a loop, thus increasing the RNA-binding surface of the protein. Surprisingly, although DDX3X was crystallized in the presence of a large excess of ADP or the slowly hydrolyzable ATP analogue ATPγS the contaminant AMP was seen in the structure. A fluorescent-based stability assay showed that the thermal stability of DDX3X was increased by the mononucleotide AMP but not by ADP or ATPγS, suggesting that DDX3X is stabilized by AMP and elucidating why AMP was found in the nucleotide-binding pocket.

Place, publisher, year, edition, pages
2007. Vol. 372, no 1, 150-159 p.
Keyword [en]
DEAD-box, helicase, HIV, nucleotide, RNA, adenosine diphosphate, adenosine phosphate, adenosine triphosphate, DEAD box protein, dead box protein ddx3x, mononucleotide amp, RNA binding protein, unclassified drug, amino acid sequence, amino terminal sequence, article, carboxy terminal sequence, crystal structure, crystallization, priority journal, Adenosine Monophosphate, Binding Sites, Conserved Sequence, Crystallography, X-Ray, DEAD-box RNA Helicases, Enzyme Stability, Humans, Hydrolysis, Models, Molecular, Molecular Sequence Data, Protein Structure, Tertiary, RNA-Binding Proteins, Sequence Homology, Amino Acid
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:sh:diva-22557DOI: 10.1016/j.jmb.2007.06.050PubMedID: 17631897Scopus ID: 2-s2.0-34547751991OAI: oai:DiVA.org:sh-22557DiVA: diva2:704606
Available from: 2014-03-12 Created: 2014-03-03 Last updated: 2014-03-12Bibliographically approved

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CiteExportLink to record
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Citation style
  • apa
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