5n9d: Difference between revisions
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The | ==Crystal Structure of Drosophila DHX36 helicase in complex with GGGTTAGGGT== | ||
<StructureSection load='5n9d' size='340' side='right' caption='[[5n9d]], [[Resolution|resolution]] 2.71Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5n9d]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N9D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N9D FirstGlance]. <br> | |||
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosinetriphosphatase Adenosinetriphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.3 3.6.1.3] </span></td></tr> | |||
<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=5n9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n9d OCA], [http://pdbe.org/5n9d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n9d RCSB], [http://www.ebi.ac.uk/pdbsum/5n9d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n9d ProSAT]</span></td></tr> | |||
</table> | |||
<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 5n9d" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Adenosinetriphosphatase]] | |||
[[Category: Chen, W F]] | |||
[[Category: Dai, Y X]] | |||
[[Category: Guo, H L]] | |||
[[Category: Liu, N N]] | |||
[[Category: Liu, Q W]] | |||
[[Category: Rety, S]] | [[Category: Rety, S]] | ||
[[Category: Wu, W Q]] | |||
[[Category: Wu, W | [[Category: Xi, X G]] | ||
[[Category: | [[Category: Helicase dexh ssdna]] | ||
[[Category: | [[Category: Hydrolase]] | ||
[[Category: | |||
Revision as of 09:19, 14 March 2018
Crystal Structure of Drosophila DHX36 helicase in complex with GGGTTAGGGTCrystal Structure of Drosophila DHX36 helicase in complex with GGGTTAGGGT
Structural highlights
Publication 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. References
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