5n90: Difference between revisions
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The | ==Crystal Structure of Drosophila DHX36 helicase in complex with TTGTGGTGT== | ||
<StructureSection load='5n90' size='340' side='right'caption='[[5n90]], [[Resolution|resolution]] 3.07Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5n90]] 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=5N90 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N90 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]] 3.069Å</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=5n90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n90 OCA], [https://pdbe.org/5n90 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n90 RCSB], [https://www.ebi.ac.uk/pdbsum/5n90 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n90 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5n90" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Helicase 3D structures|Helicase 3D structures]] | ||
[[Category: Guo | == References == | ||
[[Category: Liu | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: Xi | </StructureSection> | ||
[[Category: Drosophila melanogaster]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen W-F]] | |||
[[Category: Dai Y-X]] | |||
[[Category: Guo H-L]] | |||
[[Category: Liu N-N]] | |||
[[Category: Liu Q-W]] | |||
[[Category: Rety S]] | |||
[[Category: Wu W-Q]] | |||
[[Category: Xi X-G]] | |||
Latest revision as of 15:37, 15 November 2023
Crystal Structure of Drosophila DHX36 helicase in complex with TTGTGGTGTCrystal Structure of Drosophila DHX36 helicase in complex with TTGTGGTGT
Structural highlights
FunctionPublication Abstract from PubMedHelicase 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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