View source for 8pjb


==Cryo-EM structure of MLE in complex with UUC RNA and ADP==
<StructureSection load='8pjb' size='340' side='right'caption='[[8pjb]], [[Resolution|resolution]] 3.62&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8pjb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8PJB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8PJB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.62&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8pjb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8pjb OCA], [https://pdbe.org/8pjb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8pjb RCSB], [https://www.ebi.ac.uk/pdbsum/8pjb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8pjb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MLE_DROME MLE_DROME] Required in males for dosage compensation of X chromosome linked genes. Mle, msl-1 and msl-3 are colocalized on X chromosome. Each of the msl proteins requires all the other msls for wild-type X-chromosome binding. Probably unwinds double-stranded DNA and RNA in a 3' to 5' direction.<ref>PMID:1653648</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
RNA unwinding by DExH-type helicases underlies most RNA metabolism and function. It remains unresolved if and how the basic unwinding reaction of helicases is regulated by auxiliary domains. We explored the interplay between the RecA and auxiliary domains of the RNA helicase maleless (MLE) from Drosophila using structural and functional studies. We discovered that MLE exists in a dsRNA-bound open conformation and that the auxiliary dsRBD2 domain aligns the substrate RNA with the accessible helicase tunnel. In an ATP-dependent manner, dsRBD2 associates with the helicase module, leading to tunnel closure around ssRNA. Furthermore, our structures provide a rationale for blunt-ended dsRNA unwinding and 3'-5' translocation by MLE. Structure-based MLE mutations confirm the functional relevance of our model for RNA unwinding. Our findings contribute to our understanding of the fundamental mechanics of auxiliary domains in DExH helicase MLE, which serves as a model for its human ortholog and potential therapeutic target, DHX9/RHA.

Structural basis of RNA-induced autoregulation of the DExH-type RNA helicase maleless.,Jagtap PKA, Muller M, Kiss AE, Thomae AW, Lapouge K, Beck M, Becker PB, Hennig J Mol Cell. 2023 Dec 7;83(23):4318-4333.e10. doi: 10.1016/j.molcel.2023.10.026. , Epub 2023 Nov 20. PMID:37989319<ref>PMID:37989319</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8pjb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Hennig J]]
[[Category: Jagtap PKA]]