3ews: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ews FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ews OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ews RCSB], [http://www.ebi.ac.uk/pdbsum/3ews PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ews FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ews OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ews RCSB], [http://www.ebi.ac.uk/pdbsum/3ews PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/DD19B_HUMAN DD19B_HUMAN]] ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19B functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 23:21, 24 December 2014
Human DEAD-box RNA-helicase DDX19 in complex with ADPHuman DEAD-box RNA-helicase DDX19 in complex with ADP
Structural highlights
Function[DD19B_HUMAN] ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19B functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDEXD/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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also
References
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- 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
- Structural genomic
- 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
- Translocation
- Transport