The DEXD/H-box RNA helicase DDX19 is regulated by an α-helical switch
Collins, Ruairi ; Karlberg, Tobias LU ; Lehtiö, Lari ; Schütz, Patrick ; van den Berg, Susanne ; Dahlgren, Lars-Göran ; Hammarström, Martin ; Weigelt, Johan and Schüler, Herwig LU
(2009)
In The Journal of biological chemistry
284(16).
p.300-10296
- Abstract
DEXD/H-box RNA helicases couple ATP hydrolysis to RNA remodeling by an unknown mechanism. We used x-ray crystallography and biochemical analysis of the human DEXD/H-box protein DDX19 to investigate its regulatory mechanism. The crystal structures of DDX19, in its RNA-bound prehydrolysis and free posthydrolysis state, reveal an alpha-helix that inserts between the conserved domains of the free protein to negatively regulate ATPase activity. This finding was corroborated by biochemical data that confirm an autoregulatory function of the N-terminal region of the protein. This is the first study describing crystal structures of a DEXD/H-box protein in its open and closed cleft conformations.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2878d825-af10-4356-960e-9e39d96c33b5
- author
- Collins, Ruairi
; Karlberg, Tobias
LU
; Lehtiö, Lari
; Schütz, Patrick
; van den Berg, Susanne
; Dahlgren, Lars-Göran
; Hammarström, Martin
; Weigelt, Johan
and Schüler, Herwig
LU
- publishing date
- 2009-04-17
- type
- Contribution to journal
- publication status
- published
- keywords
- Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, DEAD-box RNA Helicases/chemistry, Humans, Models, Molecular, Molecular Sequence Data, Nucleocytoplasmic Transport Proteins/chemistry, Protein Structure, Secondary, Protein Structure, Tertiary
- in
- The Journal of biological chemistry
- volume
- 284
- issue
- 16
- pages
- 5 pages
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:19244245
- scopus:67449105353
- ISSN
- 0021-9258
- DOI
- 10.1074/jbc.C900018200
- language
- English
- LU publication?
- no
- id
- 2878d825-af10-4356-960e-9e39d96c33b5
- date added to LUP
- 2024-11-21 18:03:15
- date last changed
- 2025-03-28 16:26:13
@article{2878d825-af10-4356-960e-9e39d96c33b5,
abstract = {{<p>DEXD/H-box RNA helicases couple ATP hydrolysis to RNA remodeling by an unknown mechanism. We used x-ray crystallography and biochemical analysis of the human DEXD/H-box protein DDX19 to investigate its regulatory mechanism. The crystal structures of DDX19, in its RNA-bound prehydrolysis and free posthydrolysis state, reveal an alpha-helix that inserts between the conserved domains of the free protein to negatively regulate ATPase activity. This finding was corroborated by biochemical data that confirm an autoregulatory function of the N-terminal region of the protein. This is the first study describing crystal structures of a DEXD/H-box protein in its open and closed cleft conformations.</p>}},
author = {{Collins, Ruairi and Karlberg, Tobias and Lehtiö, Lari and Schütz, Patrick and van den Berg, Susanne and Dahlgren, Lars-Göran and Hammarström, Martin and Weigelt, Johan and Schüler, Herwig}},
issn = {{0021-9258}},
keywords = {{Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; DEAD-box RNA Helicases/chemistry; Humans; Models, Molecular; Molecular Sequence Data; Nucleocytoplasmic Transport Proteins/chemistry; Protein Structure, Secondary; Protein Structure, Tertiary}},
language = {{eng}},
month = {{04}},
number = {{16}},
pages = {{300--10296}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{The Journal of biological chemistry}},
title = {{The DE<i>X</i>D/H-box RNA helicase DDX19 is regulated by an α-helical switch}},
url = {{http://dx.doi.org/10.1074/jbc.C900018200}},
doi = {{10.1074/jbc.C900018200}},
volume = {{284}},
year = {{2009}},
}