3g0h
From Proteopedia
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===Human dead-box RNA helicase DDX19, in complex with an ATP-analogue and RNA=== | ===Human dead-box RNA helicase DDX19, in complex with an ATP-analogue and RNA=== | ||
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==See Also== | ==See Also== | ||
- | *[[DEAD-box RNA-helicase DDX19 in complex with ADP|DEAD-box RNA-helicase DDX19 in complex with ADP]] | ||
- | *[[Dead-box RNA helicase DDX19%2C in complex with an ATP-analogue and RNA|Dead-box RNA helicase DDX19%2C in complex with an ATP-analogue and RNA]] | ||
*[[Helicase|Helicase]] | *[[Helicase|Helicase]] | ||
- | *[[Morphs|Morphs]] | ||
- | *[[User:Wayne Decatur|User:Wayne Decatur]] | ||
- | *[[User:Wayne Decatur/3ewsSLASH3g0h Morph methods|User:Wayne Decatur/3ewsSLASH3g0h Morph methods]] | ||
- | *[[User:Wayne Decatur/3fpn Morph methods|User:Wayne Decatur/3fpn Morph methods]] | ||
==Reference== | ==Reference== |
Revision as of 11:42, 25 July 2012
Contents |
Human dead-box RNA helicase DDX19, in complex with an ATP-analogue and RNA
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
3g0h is a 2 chain structure of Helicase with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
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 | Arrowsmith, C H. | Berg, S Van Den. | 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. | Persson, C. | SGC, Structural Genomics Consortium. | Sagemark, J. | Schuler, H. | Schutz, P. | Siponen, M I. | Thorsell, A G. | Tresaugues, L. | Weigelt, J. | Welin, M. | Wisniewska, M. | Atp-binding | Dbp5 | Helicase | Hydrolase | Hydrolase-rna complex | Membrane | Mrna transport | Nuclear pore complex | Nucleotide-binding | Nucleus | Phosphoprotein | Polyuracil | Protein transport | Protein-rna complex | Rna-binding | Sgc | Structural genomic | Structural genomics consortium | Translocation | Transport