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New page: left|200px<br /> <applet load="2rb4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2rb4, resolution 2.80Å" /> '''Crystal structure o... |
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== | ==Crystal structure of the Helicase domain of human DDX25 RNA helicase== | ||
<StructureSection load='2rb4' size='340' side='right'caption='[[2rb4]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2rb4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2g2j 2g2j]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RB4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RB4 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]] 2.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2rb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rb4 OCA], [https://pdbe.org/2rb4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rb4 RCSB], [https://www.ebi.ac.uk/pdbsum/2rb4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rb4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DDX25_HUMAN DDX25_HUMAN] ATP-dependent RNA helicase. Required for mRNA export and translation regulation during spermatid development (By similarity).<ref>PMID:10608860</ref> | |||
== 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/rb/2rb4_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=2rb4 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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2rb4" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Helicase 3D structures|Helicase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Arrowsmith | [[Category: Arrowsmith CH]] | ||
[[Category: Berglund H]] | |||
[[Category: Berglund | [[Category: Edwards AM]] | ||
[[Category: Edwards | [[Category: Ehn M]] | ||
[[Category: Ehn | [[Category: Flodin S]] | ||
[[Category: Flodin | [[Category: Flores A]] | ||
[[Category: Flores | [[Category: Graslund S]] | ||
[[Category: Graslund | [[Category: Hallberg BM]] | ||
[[Category: Hallberg | [[Category: Hammarstrom M]] | ||
[[Category: Hammarstrom | [[Category: Hogbom M]] | ||
[[Category: Hogbom | [[Category: Holmberg-Schiavone L]] | ||
[[Category: Holmberg-Schiavone | [[Category: Kotenyova T]] | ||
[[Category: Kotenyova | [[Category: Lehtio L]] | ||
[[Category: Lehtio | [[Category: Nilsson-Ehle P]] | ||
[[Category: Nilsson-Ehle | [[Category: Nordlund P]] | ||
[[Category: Nordlund | [[Category: Nyman T]] | ||
[[Category: Nyman | [[Category: Ogg D]] | ||
[[Category: Ogg | [[Category: Persson C]] | ||
[[Category: Persson | [[Category: Sagemark J]] | ||
[[Category: Stenmark P]] | |||
[[Category: Sagemark | [[Category: Sundstrom M]] | ||
[[Category: Stenmark | [[Category: Thorsell AG]] | ||
[[Category: Sundstrom | [[Category: Uppenberg J]] | ||
[[Category: Thorsell | [[Category: Van den Berg S]] | ||
[[Category: Uppenberg | [[Category: Weigelt J]] | ||
[[Category: | |||
[[Category: | |||
Latest revision as of 14:52, 30 August 2023
Crystal structure of the Helicase domain of human DDX25 RNA helicaseCrystal structure of the Helicase domain of human DDX25 RNA helicase
Structural highlights
FunctionDDX25_HUMAN ATP-dependent RNA helicase. Required for mRNA export and translation regulation during spermatid development (By similarity).[1] 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 PubMedDEAD-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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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