3ews: Difference between revisions
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==Human DEAD-box RNA-helicase DDX19 in complex with ADP== | |||
<StructureSection load='3ews' size='340' side='right' caption='[[3ews]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EWS FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DBP5, DDX19, DDX19B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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> | |||
== 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/chain_selection.php?pdb_ID=2ata 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
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*[[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]] | *[[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]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Andersson,j | [[Category: Andersson,j]] | ||
[[Category: Arrowsmith,c h | [[Category: Arrowsmith,c h]] | ||
[[Category: Berglund,h | [[Category: Berglund,h]] | ||
[[Category: Bountra, c | [[Category: Bountra, c]] | ||
[[Category: Collins,r | [[Category: Collins,r]] | ||
[[Category: Dahlgren,l g | [[Category: Dahlgren,l g]] | ||
[[Category: Edwards,a m | [[Category: Edwards,a m]] | ||
[[Category: Flodin,s | [[Category: Flodin,s]] | ||
[[Category: Flores,a | [[Category: Flores,a]] | ||
[[Category: Graslund,s | [[Category: Graslund,s]] | ||
[[Category: Hammarstrom,m | [[Category: Hammarstrom,m]] | ||
[[Category: Johansson,a | [[Category: Johansson,a]] | ||
[[Category: Johansson,i | [[Category: Johansson,i]] | ||
[[Category: Karlberg,t | [[Category: Karlberg,t]] | ||
[[Category: Kotenyova,t | [[Category: Kotenyova,t]] | ||
[[Category: Lehtio,l | [[Category: Lehtio,l]] | ||
[[Category: Moche,m | [[Category: Moche,m]] | ||
[[Category: Nilsson,m e | [[Category: Nilsson,m e]] | ||
[[Category: Nordlund,p | [[Category: Nordlund,p]] | ||
[[Category: Nyman,t | [[Category: Nyman,t]] | ||
[[Category: Olesen,k | [[Category: Olesen,k]] | ||
[[Category: Persson,c | [[Category: Persson,c]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Sagemark,j | [[Category: Sagemark,j]] | ||
[[Category: Schueler,h | [[Category: Schueler,h]] | ||
[[Category: Thorsell,a g | [[Category: Thorsell,a g]] | ||
[[Category: Tresaugues,l | [[Category: Tresaugues,l]] | ||
[[Category: Weigelt, j | [[Category: Weigelt, j]] | ||
[[Category: Welin,m | [[Category: Welin,m]] | ||
[[Category: Wikstrom,m | [[Category: Wikstrom,m]] | ||
[[Category: Wisniewska,m | [[Category: Wisniewska,m]] | ||
[[Category: Berg, s Van den | [[Category: Berg, s Van den]] | ||
[[Category: Adp]] | [[Category: Adp]] | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
Line 62: | Line 83: | ||
[[Category: Rrna]] | [[Category: Rrna]] | ||
[[Category: Sgc]] | [[Category: Sgc]] | ||
[[Category: Translocation]] | [[Category: Translocation]] | ||
[[Category: Transport]] | [[Category: Transport]] |
Revision as of 16:51, 17 December 2014
Human DEAD-box RNA-helicase DDX19 in complex with ADPHuman DEAD-box RNA-helicase DDX19 in complex with ADP
Structural highlights
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