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[[Image:2pl3.jpg|left|200px]]


{{Structure
==Human DEAD-box RNA helicase DDX10, DEAD domain in complex with ADP==
|PDB= 2pl3 |SIZE=350|CAPTION= <scene name='initialview01'>2pl3</scene>, resolution 2.15&Aring;
<StructureSection load='2pl3' size='340' side='right'caption='[[2pl3]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
|SITE=
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>
<table><tr><td colspan='2'>[[2pl3]] is a 1 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=2PL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PL3 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
|GENE= DDX10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<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>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2pl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pl3 OCA], [https://pdbe.org/2pl3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pl3 RCSB], [https://www.ebi.ac.uk/pdbsum/2pl3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pl3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DDX10_HUMAN DDX10_HUMAN] Putative ATP-dependent RNA helicase.
== 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/pl/2pl3_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=2pl3 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
DEAD-box RNA helicases play various, often critical, roles in all processes where RNAs are involved. Members of this family of proteins are linked to human disease, including cancer and viral infections. DEAD-box proteins contain two conserved domains that both contribute to RNA and ATP binding. Despite recent advances the molecular details of how these enzymes convert chemical energy into RNA remodeling is unknown. We present crystal structures of the isolated DEAD-domains of human DDX2A/eIF4A1, DDX2B/eIF4A2, DDX5, DDX10/DBP4, DDX18/myc-regulated DEAD-box protein, DDX20, DDX47, DDX52/ROK1, and DDX53/CAGE, and of the helicase domains of DDX25 and DDX41. Together with prior knowledge this enables a family-wide comparative structural analysis. We propose a general mechanism for opening of the RNA binding site. This analysis also provides insights into the diversity of DExD/H- proteins, with implications for understanding the functions of individual family members.


'''Human DEAD-box RNA helicase DDX10, DEAD domain in complex with ADP'''
Comparative structural analysis of human DEAD-box RNA helicases.,Schutz P, Karlberg T, van den Berg S, Collins R, Lehtio L, Hogbom M, Holmberg-Schiavone L, Tempel W, Park HW, Hammarstrom M, Moche M, Thorsell AG, Schuler H PLoS One. 2010 Sep 30;5(9). pii: e12791. PMID:20941364<ref>PMID:20941364</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2pl3" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
2PL3 is a [[Single protein]] structure of 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=2PL3 OCA].
*[[Helicase 3D structures|Helicase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H.]]
[[Category: Arrowsmith CH]]
[[Category: Berg, S Van Den.]]
[[Category: Berglund H]]
[[Category: Berglund, H.]]
[[Category: Busam RD]]
[[Category: Busam, R D.]]
[[Category: Collins R]]
[[Category: Collins, R.]]
[[Category: Dahlgren LG]]
[[Category: Dahlgren, L G.]]
[[Category: Edwards A]]
[[Category: Edwards, A.]]
[[Category: Flodin S]]
[[Category: Flodin, S.]]
[[Category: Flores A]]
[[Category: Flores, A.]]
[[Category: Graslund S]]
[[Category: Graslund, S.]]
[[Category: Hallberg BM]]
[[Category: Hallberg, B M.]]
[[Category: Hammarstrom M]]
[[Category: Hammarstrom, M.]]
[[Category: Holmberg-Schiavone L]]
[[Category: Holmberg-Schiavone, L.]]
[[Category: Johansson I]]
[[Category: Johansson, I.]]
[[Category: Kallas A]]
[[Category: Kallas, A.]]
[[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: Nordlund P]]
[[Category: Nordlund, P.]]
[[Category: Nyman T]]
[[Category: Nyman, T.]]
[[Category: Persson C]]
[[Category: Persson, C.]]
[[Category: Sagemark J]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Stenmark P]]
[[Category: Sagemark, J.]]
[[Category: Sundstrom M]]
[[Category: Stenmark, P.]]
[[Category: Thorsell AG]]
[[Category: Sundstrom, M.]]
[[Category: Van Den Berg S]]
[[Category: Thorsell, A G.]]
[[Category: Weigelt J]]
[[Category: Weigelt, J.]]
[[Category: ADP]]
[[Category: EOH]]
[[Category: MG]]
[[Category: dead]]
[[Category: helicase]]
[[Category: rna]]
[[Category: sgc]]
[[Category: structural genomic]]
[[Category: structural genomics consortium]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:14:20 2008''

Latest revision as of 14:03, 30 August 2023

Human DEAD-box RNA helicase DDX10, DEAD domain in complex with ADPHuman DEAD-box RNA helicase DDX10, DEAD domain in complex with ADP

Structural highlights

2pl3 is a 1 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 2.15Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DDX10_HUMAN Putative ATP-dependent RNA helicase.

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

DEAD-box RNA helicases play various, often critical, roles in all processes where RNAs are involved. Members of this family of proteins are linked to human disease, including cancer and viral infections. DEAD-box proteins contain two conserved domains that both contribute to RNA and ATP binding. Despite recent advances the molecular details of how these enzymes convert chemical energy into RNA remodeling is unknown. We present crystal structures of the isolated DEAD-domains of human DDX2A/eIF4A1, DDX2B/eIF4A2, DDX5, DDX10/DBP4, DDX18/myc-regulated DEAD-box protein, DDX20, DDX47, DDX52/ROK1, and DDX53/CAGE, and of the helicase domains of DDX25 and DDX41. Together with prior knowledge this enables a family-wide comparative structural analysis. We propose a general mechanism for opening of the RNA binding site. This analysis also provides insights into the diversity of DExD/H- proteins, with implications for understanding the functions of individual family members.

Comparative structural analysis of human DEAD-box RNA helicases.,Schutz P, Karlberg T, van den Berg S, Collins R, Lehtio L, Hogbom M, Holmberg-Schiavone L, Tempel W, Park HW, Hammarstrom M, Moche M, Thorsell AG, Schuler H PLoS One. 2010 Sep 30;5(9). pii: e12791. PMID:20941364[1]

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

See Also

References

  1. ↑ Schutz P, Karlberg T, van den Berg S, Collins R, Lehtio L, Hogbom M, Holmberg-Schiavone L, Tempel W, Park HW, Hammarstrom M, Moche M, Thorsell AG, Schuler H. Comparative structural analysis of human DEAD-box RNA helicases. PLoS One. 2010 Sep 30;5(9). pii: e12791. PMID:20941364 doi:10.1371/journal.pone.0012791

2pl3, resolution 2.15Å

Drag the structure with the mouse to rotate

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