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[[Image:3ews.png|left|200px]]


{{STRUCTURE_3ews| PDB=3ews | SCENE= }}
==Human DEAD-box RNA-helicase DDX19 in complex with ADP==
<StructureSection load='3ews' size='340' side='right'caption='[[3ews]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ews]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EWS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ews FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ews OCA], [https://pdbe.org/3ews PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ews RCSB], [https://www.ebi.ac.uk/pdbsum/3ews PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ews ProSAT]</span></td></tr>
</table>
== Function ==
[https://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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ew/3ews_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ews ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


===Human DEAD-box RNA-helicase DDX19 in complex with ADP===
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<ref>PMID:19244245</ref>


{{ABSTRACT_PUBMED_19244245}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 3ews" style="background-color:#fffaf0;"></div>
[[3ews]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EWS OCA].


==See Also==
==See Also==
*[[DEAD-box RNA-helicase DDX19 in complex with ADP|DEAD-box RNA-helicase DDX19 in complex with ADP]]
*[[Helicase 3D structures|Helicase 3D structures]]
*[[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]]
== References ==
*[[Helicase|Helicase]]
<references/>
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:019244245</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Andersson,j.]]
[[Category: Large Structures]]
[[Category: Arrowsmith,c h.]]
[[Category: Andersson j]]
[[Category: Berglund,h.]]
[[Category: Arrowsmith ch]]
[[Category: Bountra, c.]]
[[Category: Berglund h]]
[[Category: Collins,r.]]
[[Category: Bountra c]]
[[Category: Dahlgren,l g.]]
[[Category: Collins r]]
[[Category: Edwards,a m.]]
[[Category: Dahlgren lg]]
[[Category: Flodin,s.]]
[[Category: Edwards am]]
[[Category: Flores,a.]]
[[Category: Flodin s]]
[[Category: Graslund,s.]]
[[Category: Flores a]]
[[Category: Hammarstrom,m.]]
[[Category: Graslund s]]
[[Category: Johansson,a.]]
[[Category: Hammarstrom m]]
[[Category: Johansson,i.]]
[[Category: Johansson a]]
[[Category: Karlberg,t.]]
[[Category: Johansson i]]
[[Category: Kotenyova,t.]]
[[Category: Karlberg t]]
[[Category: Lehtio,l.]]
[[Category: Kotenyova t]]
[[Category: Moche,m.]]
[[Category: Lehtio l]]
[[Category: Nilsson,m e.]]
[[Category: Moche m]]
[[Category: Nordlund,p.]]
[[Category: Nilsson me]]
[[Category: Nyman,t.]]
[[Category: Nordlund p]]
[[Category: Olesen,k.]]
[[Category: Nyman t]]
[[Category: Persson,c.]]
[[Category: Olesen k]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Persson c]]
[[Category: Sagemark,j.]]
[[Category: Sagemark j]]
[[Category: Schueler,h.]]
[[Category: Schueler h]]
[[Category: Thorsell,a g.]]
[[Category: Thorsell ag]]
[[Category: Tresaugues,l.]]
[[Category: Tresaugues l]]
[[Category: Weigelt, j.]]
[[Category: Van den berg s]]
[[Category: Welin,m.]]
[[Category: Weigelt j]]
[[Category: Wikstrom,m.]]
[[Category: Welin m]]
[[Category: Wisniewska,m.]]
[[Category: Wikstrom m]]
[[Category: Berg, s Van den.]]
[[Category: Wisniewska m]]
[[Category: Adp]]
[[Category: Atp-binding]]
[[Category: Dead]]
[[Category: Helicase]]
[[Category: Hydrolase]]
[[Category: Membrane]]
[[Category: Mrna]]
[[Category: Mrna transport]]
[[Category: Nuclear pore complex]]
[[Category: Nucleotide-binding]]
[[Category: Nucleus]]
[[Category: Protein transport]]
[[Category: Rna helicase]]
[[Category: Rna-binding]]
[[Category: Rrna]]
[[Category: Sgc]]
[[Category: Structural genomic]]
[[Category: Structural genomics consortium]]
[[Category: Translocation]]
[[Category: Transport]]

Latest revision as of 03:25, 28 December 2023

Human DEAD-box RNA-helicase DDX19 in complex with ADPHuman DEAD-box RNA-helicase DDX19 in complex with ADP

Structural highlights

3ews is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ 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

3ews, resolution 2.70Å

Drag the structure with the mouse to rotate

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