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  • Högbom, MartinStockholms universitet,Institutionen för biokemi och biofysik (author)

Crystal Structure of Conserved Domains 1 and 2 of the Human DEAD-box Helicase DDX3X in Complex with the Mononucleotide AMP

  • Article/chapterEnglish2007

Publisher, publication year, extent ...

  • Elsevier BV,2007
  • printrdacarrier

Numbers

  • LIBRIS-ID:oai:DiVA.org:sh-22557
  • https://urn.kb.se/resolve?urn=urn:nbn:se:sh:diva-22557URI
  • https://doi.org/10.1016/j.jmb.2007.06.050DOI
  • https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-19855URI
  • http://kipublications.ki.se/Default.aspx?queryparsed=id:115889040URI

Supplementary language notes

  • Language:English
  • Summary in:English

Part of subdatabase

Classification

  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

Notes

  • 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.

Subject headings and genre

  • NATURVETENSKAP Biologi hsv//swe
  • NATURAL SCIENCES Biological Sciences hsv//eng
  • 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

Added entries (persons, corporate bodies, meetings, titles ...)

  • Collins, R.Karolinska Institutet (author)
  • van den Berg, S.Karolinska Institutet (author)
  • Jenvert, Rose-MarieSödertörns högskola,Institutionen för livsvetenskaper(Swepub:sh)SH99REKN (author)
  • Karlberg, T.Karolinska Institutet (author)
  • Kotenyova, T. (author)
  • Flores, A. (author)
  • Hedestam, G. B. K.Karolinska Institutet (author)
  • Schiavone, L. H. (author)
  • Stockholms universitetInstitutionen för biokemi och biofysik (creator_code:org_t)

Related titles

  • In:Journal of Molecular Biology: Elsevier BV372:1, s. 150-1590022-28361089-8638

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