5n8s: Difference between revisions

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'''Unreleased structure'''


The entry 5n8s is ON HOLD
==Crystal Structure of Drosophila DHX36 helicase in complex with polyT==
<StructureSection load='5n8s' size='340' side='right'caption='[[5n8s]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5n8s]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N8S 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]] 2.88&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5n8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n8s OCA], [https://pdbe.org/5n8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n8s RCSB], [https://www.ebi.ac.uk/pdbsum/5n8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n8s ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8SWT2_DROME Q8SWT2_DROME]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Helicase DHX36 plays essential roles in cell development and differentiation at least partially by resolving G-quadruplex (G4) structures. Here we report crystal structures of the Drosophila homolog of DHX36 (DmDHX36) in complex with RNA and a series of DNAs. By combining structural, small-angle X-ray scattering, molecular dynamics simulation, and single-molecule fluorescence studies, we revealed that positively charged amino acids in RecA2 and OB-like domains constitute an elaborate structural pocket at the nucleic acid entrance, in which negatively charged G4 DNA is tightly bound and partially destabilized. The G4 DNA is then completely unfolded through the 3'-5' translocation activity of the helicase. Furthermore, crystal structures and DNA binding assays show that G-rich DNA is preferentially recognized and in the presence of ATP, specifically bound by DmDHX36, which may cooperatively enhance the G-rich DNA translocation and G4 unfolding. On the basis of these results, a conceptual G4 DNA-resolving mechanism is proposed.


Authors: Chen, W.-F., Rety, S., Hai-Lei Guo, H.-L., Wu, W.-Q., Liu, N.-N., Liu, Q.-W., Dai, Y.-X., Xi, X.-G.
Molecular Mechanistic Insights into Drosophila DHX36-Mediated G-Quadruplex Unfolding: A Structure-Based Model.,Chen WF, Rety S, Guo HL, Dai YX, Wu WQ, Liu NN, Auguin D, Liu QW, Hou XM, Dou SX, Xi XG Structure. 2018 Mar 6;26(3):403-415.e4. doi: 10.1016/j.str.2018.01.008. Epub 2018, Feb 8. PMID:29429875<ref>PMID:29429875</ref>


Description: Crystal Structure of Drosophila DHX36 helicase in complex with polyT
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Hai-Lei Guo, H.-L]]
<div class="pdbe-citations 5n8s" style="background-color:#fffaf0;"></div>
[[Category: Xi, X.-G]]
 
[[Category: Chen, W.-F]]
==See Also==
[[Category: Rety, S]]
*[[Helicase 3D structures|Helicase 3D structures]]
[[Category: Liu, N.-N]]
== References ==
[[Category: Wu, W.-Q]]
<references/>
[[Category: Liu, Q.-W]]
__TOC__
[[Category: Dai, Y.-X]]
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chen W-F]]
[[Category: Dai Y-X]]
[[Category: Hai-Lei Guo H-L]]
[[Category: Liu N-N]]
[[Category: Liu Q-W]]
[[Category: Rety S]]
[[Category: Wu W-Q]]
[[Category: Xi X-G]]

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