6up4: Difference between revisions
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==Crystal structure of the murine DHX36 helicase in complex with ADP== | ==Crystal structure of the murine DHX36 helicase in complex with ADP== | ||
<StructureSection load='6up4' size='340' side='right'caption='[[6up4]]' scene=''> | <StructureSection load='6up4' size='340' side='right'caption='[[6up4]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UP4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UP4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6up4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UP4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UP4 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6up4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6up4 OCA], [http://pdbe.org/6up4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6up4 RCSB], [http://www.ebi.ac.uk/pdbsum/6up4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6up4 ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dhx36 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6up4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6up4 OCA], [http://pdbe.org/6up4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6up4 RCSB], [http://www.ebi.ac.uk/pdbsum/6up4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6up4 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The DEAH/RHA helicase DHX36 has been linked to cellular RNA and DNA quadruplex structures and to AU-rich RNA elements. In vitro, DHX36 remodels DNA and RNA quadruplex structures and unwinds DNA duplexes in an ATP-dependent manner. DHX36 contains the superfamily 2 helicase core and several auxiliary domains that are conserved in orthologs of the enzyme. The role of these auxiliary domains for the enzymatic function of DHX36 is not well understood. Here, we combine structural and biochemical studies to define the function of three auxiliary domains that contact nucleic acid. We first report the crystal structure of mouse DHX36 bound to ADP. The structure reveals an overall architecture of mouse DHX36 that is similar to previously reported architectures of fly and bovine DHX36. In addition, our structure shows conformational changes that accompany stages of the ATP-binding and hydrolysis cycle. We then examine the roles of the DHX36-specific motif (DSM), the OB-fold, and a conserved beta-hairpin (beta-HP) in mouse DHX36 in the remodeling of RNA structures. We demonstrate and characterize RNA duplex unwinding for DHX36 and examine the remodeling of inter- and intramolecular RNA quadruplex structures. We find that the DSM not only functions as a quadruplex binding adaptor but also promotes the remodeling of RNA duplex and quadruplex structures. The OB-fold and the beta-HP contribute to RNA binding. Both domains are also essential for remodeling RNA quadruplex and duplex structures. Our data reveal roles of auxiliary domains for multiple steps of the nucleic acid remodeling reactions. | |||
Function of Auxiliary Domains of the DEAH/RHA Helicase DHX36 in RNA Remodeling.,Srinivasan S, Liu Z, Chuenchor W, Xiao TS, Jankowsky E J Mol Biol. 2020 Feb 19. pii: S0022-2836(20)30155-8. doi:, 10.1016/j.jmb.2020.02.005. PMID:32087197<ref>PMID:32087197</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6up4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Liu Z]] | [[Category: Lk3 transgenic mice]] | ||
[[Category: Xiao | [[Category: Liu, Z]] | ||
[[Category: Xiao, T S]] | |||
[[Category: Atp-dependent]] | |||
[[Category: Dna-binding]] | |||
[[Category: G4 resolvase]] | |||
[[Category: Helicase]] | |||
[[Category: Rna binding protein]] | |||
[[Category: Rna-binding]] | |||
Revision as of 10:33, 27 May 2020
Crystal structure of the murine DHX36 helicase in complex with ADPCrystal structure of the murine DHX36 helicase in complex with ADP
Structural highlights
Publication Abstract from PubMedThe DEAH/RHA helicase DHX36 has been linked to cellular RNA and DNA quadruplex structures and to AU-rich RNA elements. In vitro, DHX36 remodels DNA and RNA quadruplex structures and unwinds DNA duplexes in an ATP-dependent manner. DHX36 contains the superfamily 2 helicase core and several auxiliary domains that are conserved in orthologs of the enzyme. The role of these auxiliary domains for the enzymatic function of DHX36 is not well understood. Here, we combine structural and biochemical studies to define the function of three auxiliary domains that contact nucleic acid. We first report the crystal structure of mouse DHX36 bound to ADP. The structure reveals an overall architecture of mouse DHX36 that is similar to previously reported architectures of fly and bovine DHX36. In addition, our structure shows conformational changes that accompany stages of the ATP-binding and hydrolysis cycle. We then examine the roles of the DHX36-specific motif (DSM), the OB-fold, and a conserved beta-hairpin (beta-HP) in mouse DHX36 in the remodeling of RNA structures. We demonstrate and characterize RNA duplex unwinding for DHX36 and examine the remodeling of inter- and intramolecular RNA quadruplex structures. We find that the DSM not only functions as a quadruplex binding adaptor but also promotes the remodeling of RNA duplex and quadruplex structures. The OB-fold and the beta-HP contribute to RNA binding. Both domains are also essential for remodeling RNA quadruplex and duplex structures. Our data reveal roles of auxiliary domains for multiple steps of the nucleic acid remodeling reactions. Function of Auxiliary Domains of the DEAH/RHA Helicase DHX36 in RNA Remodeling.,Srinivasan S, Liu Z, Chuenchor W, Xiao TS, Jankowsky E J Mol Biol. 2020 Feb 19. pii: S0022-2836(20)30155-8. doi:, 10.1016/j.jmb.2020.02.005. PMID:32087197[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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