3iuy

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Current revision (10:06, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3iuy' size='340' side='right'caption='[[3iuy]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3iuy' size='340' side='right'caption='[[3iuy]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3iuy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IUY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3iuy]] 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=3IUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IUY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.4&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDX53, CAGE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=3iuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iuy OCA], [https://pdbe.org/3iuy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iuy RCSB], [https://www.ebi.ac.uk/pdbsum/3iuy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iuy ProSAT]</span></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=3iuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iuy OCA], [https://pdbe.org/3iuy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iuy RCSB], [https://www.ebi.ac.uk/pdbsum/3iuy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iuy ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DDX53_HUMAN DDX53_HUMAN]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=3iuy ConSurf].
</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=3iuy 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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==See Also==
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*[[Helicase 3D structures|Helicase 3D structures]]
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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>
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<div class="pdbe-citations 3iuy" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Berg, S Van Den]]
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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 AM]]
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[[Category: Edwards, A M]]
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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 TK]]
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[[Category: Nielsen, T K]]
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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 AK]]
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[[Category: Roos, A K]]
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[[Category: Schuler HM]]
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[[Category: Structural genomic]]
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[[Category: Schutz P]]
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[[Category: Schuler, H M]]
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[[Category: Siponen MI]]
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[[Category: Schutz, P]]
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[[Category: Svensson L]]
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[[Category: Siponen, M I]]
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[[Category: Thorsell AG]]
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[[Category: Svensson, L]]
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[[Category: Tresaugues L]]
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[[Category: Thorsell, A G]]
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[[Category: Van Den Berg S]]
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[[Category: Tresaugues, L]]
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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: Atp-binding]]
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[[Category: Dead-box]]
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[[Category: Helicase]]
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[[Category: Hydrolase]]
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[[Category: Nucleotide-binding]]
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[[Category: Nucleus]]
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[[Category: Rec-a-like]]
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[[Category: Rna-binding]]
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[[Category: Sgc]]
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Current revision

Crystal structure of DDX53 DEAD-box domain

PDB ID 3iuy

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Proteopedia Page Contributors and Editors (what is this?)

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