3ews
From Proteopedia
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{{STRUCTURE_3ews| PDB=3ews | SCENE= }} | {{STRUCTURE_3ews| PDB=3ews | SCENE= }} | ||
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===Human DEAD-box RNA-helicase DDX19 in complex with ADP=== | ===Human DEAD-box RNA-helicase DDX19 in complex with ADP=== | ||
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{{ABSTRACT_PUBMED_19244245}} | {{ABSTRACT_PUBMED_19244245}} | ||
Revision as of 09:42, 11 March 2013
Contents |
Human DEAD-box RNA-helicase DDX19 in complex with ADP
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.
The DEXD/H-box RNA helicase DDX19 is regulated by an {alpha}-helical switch., Collins R, Karlberg T, Lehtio L, Schutz P, van den Berg S, Dahlgren LG, Hammarstrom M, Weigelt J, Schuler H, J Biol Chem. 2009 Apr 17;284(16):10296-300. Epub 2009 Feb 25. PMID:19244245
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
3ews is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
- DEAD-box RNA-helicase DDX19 in complex with ADP
- Dead-box RNA helicase DDX19%2C in complex with an ATP-analogue and RNA
- Helicase
Reference
- Collins R, Karlberg T, Lehtio L, Schutz P, van den Berg S, Dahlgren LG, Hammarstrom M, Weigelt J, Schuler H. The DEXD/H-box RNA helicase DDX19 is regulated by an {alpha}-helical switch. J Biol Chem. 2009 Apr 17;284(16):10296-300. Epub 2009 Feb 25. PMID:19244245 doi:10.1074/jbc.C900018200
Categories: Homo sapiens | Andersson,j. | Arrowsmith,c h. | Berglund,h. | Bountra, c. | Collins,r. | Dahlgren,l g. | Edwards,a m. | Flodin,s. | Flores,a. | Graslund,s. | Hammarstrom,m. | Johansson,a. | Johansson,i. | Karlberg,t. | Kotenyova,t. | Lehtio,l. | Moche,m. | Nilsson,m e. | Nordlund,p. | Nyman,t. | Olesen,k. | Persson,c. | SGC, Structural Genomics Consortium. | Sagemark,j. | Schueler,h. | Thorsell,a g. | Tresaugues,l. | Weigelt, j. | Welin,m. | Wikstrom,m. | Wisniewska,m. | Berg, s Van den. | Adp | Atp-binding | Dead | Helicase | Hydrolase | Membrane | Mrna | Mrna transport | Nuclear pore complex | Nucleotide-binding | Nucleus | Protein transport | Rna helicase | Rna-binding | Rrna | Sgc | Structural genomic | Structural genomics consortium | Translocation | Transport
