6f3h: Difference between revisions
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==Crystal structure of Dss1 exoribonuclease active site mutant D477N from Candida glabrata== | ==Crystal structure of Dss1 exoribonuclease active site mutant D477N from Candida glabrata== | ||
<StructureSection load='6f3h' size='340' side='right' caption='[[6f3h]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='6f3h' size='340' side='right'caption='[[6f3h]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6f3h]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6f3h]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)] and [https://en.wikipedia.org/wiki/Candida_glabrata Candida glabrata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F3H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6F3H FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.703Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6f3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f3h OCA], [https://pdbe.org/6f3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6f3h RCSB], [https://www.ebi.ac.uk/pdbsum/6f3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6f3h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6FJE0_CANGA Q6FJE0_CANGA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Nowak E]] | ||
[[Category: | [[Category: Nowotny M]] | ||
[[Category: | [[Category: Razew M]] | ||
Latest revision as of 08:12, 21 November 2024
Crystal structure of Dss1 exoribonuclease active site mutant D477N from Candida glabrataCrystal structure of Dss1 exoribonuclease active site mutant D477N from Candida glabrata
Structural highlights
FunctionPublication Abstract from PubMedNuclease and helicase activities play pivotal roles in various aspects of RNA processing and degradation. These two activities are often present in multi-subunit complexes from nucleic acid metabolism. In the mitochondrial exoribonuclease complex (mtEXO) both enzymatic activities are tightly coupled making it an excellent minimal system to study helicase-exoribonuclease coordination. mtEXO is composed of Dss1 3'-to-5' exoribonuclease and Suv3 helicase. It is the master regulator of mitochondrial gene expression in yeast. Here, we present the structure of mtEXO and a description of its mechanism of action. The crystal structure of Dss1 reveals domains that are responsible for interactions with Suv3. Importantly, these interactions are compatible with the conformational changes of Suv3 domains during the helicase cycle. We demonstrate that mtEXO is an intimate complex which forms an RNA-binding channel spanning its entire structure, with Suv3 helicase feeding the 3' end of the RNA toward the active site of Dss1. Structural analysis of mtEXO mitochondrial RNA degradosome reveals tight coupling of nuclease and helicase components.,Razew M, Warkocki Z, Taube M, Kolondra A, Czarnocki-Cieciura M, Nowak E, Labedzka-Dmoch K, Kawinska A, Piatkowski J, Golik P, Kozak M, Dziembowski A, Nowotny M Nat Commun. 2018 Jan 8;9(1):97. doi: 10.1038/s41467-017-02570-5. PMID:29311576[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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