3ly5

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==DDX18 dead-domain==
==DDX18 dead-domain==
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<StructureSection load='3ly5' size='340' side='right' caption='[[3ly5]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='3ly5' size='340' side='right'caption='[[3ly5]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ly5]] 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=3LY5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LY5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ly5]] 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=3LY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LY5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDX18 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr>
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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=3ly5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ly5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ly5 RCSB], [http://www.ebi.ac.uk/pdbsum/3ly5 PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ly5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ly5 OCA], [https://pdbe.org/3ly5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ly5 RCSB], [https://www.ebi.ac.uk/pdbsum/3ly5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ly5 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DDX18_HUMAN DDX18_HUMAN] Probable RNA-dependent helicase.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ly/3ly5_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ly/3ly5_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</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].
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</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=3ly5 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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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>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
==See Also==
==See Also==
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*[[Helicase|Helicase]]
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*[[Helicase 3D structures|Helicase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Arrowsmith, C H]]
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[[Category: Large Structures]]
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[[Category: Berg, S Van Den]]
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[[Category: Arrowsmith CH]]
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[[Category: Berglund, H]]
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[[Category: Berglund H]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Collins, R]]
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[[Category: Collins R]]
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[[Category: Edwards, A M]]
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[[Category: Edwards AM]]
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[[Category: Flodin, S]]
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[[Category: Flodin S]]
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[[Category: Flores, A]]
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[[Category: Flores A]]
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[[Category: Graslund, S]]
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[[Category: Graslund S]]
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[[Category: Hammarstrom, M]]
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[[Category: Hammarstrom M]]
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[[Category: Johansson, A]]
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[[Category: Johansson A]]
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[[Category: Johansson, I]]
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[[Category: Johansson I]]
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[[Category: Kallas, A]]
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[[Category: Kallas A]]
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[[Category: Karlberg, T]]
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[[Category: Karlberg T]]
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[[Category: Kotenyova, T]]
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[[Category: Kotenyova T]]
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[[Category: Kotzsch, A]]
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[[Category: Kotzsch A]]
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[[Category: Kraulis, P]]
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[[Category: Kraulis P]]
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[[Category: Markova, N]]
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[[Category: Markova N]]
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[[Category: Moche, M]]
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[[Category: Moche M]]
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[[Category: Nielsen, T K]]
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[[Category: Nielsen TK]]
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[[Category: Nordlund, P]]
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[[Category: Nordlund P]]
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[[Category: Nyman, T]]
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[[Category: Nyman T]]
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[[Category: Persson, C]]
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[[Category: Persson C]]
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[[Category: Roos, A K]]
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[[Category: Roos AK]]
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[[Category: Structural genomic]]
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[[Category: Schuler HM]]
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[[Category: Schuler, H M]]
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[[Category: Schutz P]]
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[[Category: Schutz, P]]
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[[Category: Siponen MI]]
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[[Category: Siponen, M I]]
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[[Category: Svensson L]]
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[[Category: Svensson, L]]
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[[Category: Thorsell AG]]
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[[Category: Thorsell, A G]]
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[[Category: Tresaugues L]]
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[[Category: Tresaugues, L]]
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[[Category: Van Den Berg S]]
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[[Category: Wahlberg, E]]
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[[Category: Wahlberg E]]
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[[Category: Weigelt, J]]
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[[Category: Weigelt J]]
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[[Category: Welin, M]]
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[[Category: Welin M]]
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[[Category: Wisniewska, M]]
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[[Category: Wisniewska M]]
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[[Category: Alpha-beta]]
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[[Category: Atp-binding]]
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[[Category: Helicase]]
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[[Category: Hydrolase]]
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[[Category: Nucleotide-binding]]
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[[Category: Rna-binding]]
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[[Category: Sgc]]
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Current revision

DDX18 dead-domain

PDB ID 3ly5

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