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Comparative structural analysis of human DEAD-box RNA helicases

Schütz, Patrick ; Karlberg, Tobias LU ; van den Berg, Susanne ; Collins, Ruairi ; Lehtiö, Lari ; Högbom, Martin ; Holmberg-Schiavone, Lovisa ; Tempel, Wolfram ; Park, Hee-Won and Hammarström, Martin , et al. (2010) In PLoS ONE 5(9).
Abstract

DEAD-box RNA helicases play various, often critical, roles in all processes where RNAs are involved. Members of this family of proteins are linked to human disease, including cancer and viral infections. DEAD-box proteins contain two conserved domains that both contribute to RNA and ATP binding. Despite recent advances the molecular details of how these enzymes convert chemical energy into RNA remodeling is unknown. We present crystal structures of the isolated DEAD-domains of human DDX2A/eIF4A1, DDX2B/eIF4A2, DDX5, DDX10/DBP4, DDX18/myc-regulated DEAD-box protein, DDX20, DDX47, DDX52/ROK1, and DDX53/CAGE, and of the helicase domains of DDX25 and DDX41. Together with prior knowledge this enables a family-wide comparative structural... (More)

DEAD-box RNA helicases play various, often critical, roles in all processes where RNAs are involved. Members of this family of proteins are linked to human disease, including cancer and viral infections. DEAD-box proteins contain two conserved domains that both contribute to RNA and ATP binding. Despite recent advances the molecular details of how these enzymes convert chemical energy into RNA remodeling is unknown. We present crystal structures of the isolated DEAD-domains of human DDX2A/eIF4A1, DDX2B/eIF4A2, DDX5, DDX10/DBP4, DDX18/myc-regulated DEAD-box protein, DDX20, DDX47, DDX52/ROK1, and DDX53/CAGE, and of the helicase domains of DDX25 and DDX41. Together with prior knowledge this enables a family-wide comparative structural analysis. We propose a general mechanism for opening of the RNA binding site. This analysis also provides insights into the diversity of DExD/H- proteins, with implications for understanding the functions of individual family members.

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publishing date
type
Contribution to journal
publication status
published
keywords
Adenosine Triphosphate/metabolism, Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, DEAD-box RNA Helicases/chemistry, Humans, Models, Molecular, Molecular Conformation, Molecular Sequence Data, Multigene Family, Protein Structure, Tertiary, RNA/metabolism, Sequence Alignment
in
PLoS ONE
volume
5
issue
9
article number
e12791
pages
11 pages
publisher
Public Library of Science (PLoS)
external identifiers
  • pmid:20941364
  • scopus:77958568836
ISSN
1932-6203
DOI
10.1371/journal.pone.0012791
language
English
LU publication?
no
id
52e4e514-b473-4df8-9e90-bd831457a727
date added to LUP
2024-11-21 18:00:11
date last changed
2025-07-19 00:27:17
@article{52e4e514-b473-4df8-9e90-bd831457a727,
  abstract     = {{<p>DEAD-box RNA helicases play various, often critical, roles in all processes where RNAs are involved. Members of this family of proteins are linked to human disease, including cancer and viral infections. DEAD-box proteins contain two conserved domains that both contribute to RNA and ATP binding. Despite recent advances the molecular details of how these enzymes convert chemical energy into RNA remodeling is unknown. We present crystal structures of the isolated DEAD-domains of human DDX2A/eIF4A1, DDX2B/eIF4A2, DDX5, DDX10/DBP4, DDX18/myc-regulated DEAD-box protein, DDX20, DDX47, DDX52/ROK1, and DDX53/CAGE, and of the helicase domains of DDX25 and DDX41. Together with prior knowledge this enables a family-wide comparative structural analysis. We propose a general mechanism for opening of the RNA binding site. This analysis also provides insights into the diversity of DExD/H- proteins, with implications for understanding the functions of individual family members.</p>}},
  author       = {{Schütz, Patrick and Karlberg, Tobias and van den Berg, Susanne and Collins, Ruairi and Lehtiö, Lari and Högbom, Martin and Holmberg-Schiavone, Lovisa and Tempel, Wolfram and Park, Hee-Won and Hammarström, Martin and Moche, Martin and Thorsell, Ann-Gerd and Schüler, Herwig}},
  issn         = {{1932-6203}},
  keywords     = {{Adenosine Triphosphate/metabolism; Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; DEAD-box RNA Helicases/chemistry; Humans; Models, Molecular; Molecular Conformation; Molecular Sequence Data; Multigene Family; Protein Structure, Tertiary; RNA/metabolism; Sequence Alignment}},
  language     = {{eng}},
  month        = {{09}},
  number       = {{9}},
  publisher    = {{Public Library of Science (PLoS)}},
  series       = {{PLoS ONE}},
  title        = {{Comparative structural analysis of human DEAD-box RNA helicases}},
  url          = {{http://dx.doi.org/10.1371/journal.pone.0012791}},
  doi          = {{10.1371/journal.pone.0012791}},
  volume       = {{5}},
  year         = {{2010}},
}