6y3p: Difference between revisions
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==Crystal structure of the C-terminal domain from K. lactis Pby1, an ATP-grasp enzyme interacting with the mRNA decapping enzyme Dcp2== | ==Crystal structure of the C-terminal domain from K. lactis Pby1, an ATP-grasp enzyme interacting with the mRNA decapping enzyme Dcp2== | ||
<StructureSection load='6y3p' size='340' side='right'caption='[[6y3p]]' scene=''> | <StructureSection load='6y3p' size='340' side='right'caption='[[6y3p]], [[Resolution|resolution]] 2.30Å' 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=6Y3P OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6Y3P FirstGlance]. <br> | <table><tr><td colspan='2'>[[6y3p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_sphaerica Candida sphaerica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y3P OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6Y3P 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=6y3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y3p OCA], [http://pdbe.org/6y3p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6y3p RCSB], [http://www.ebi.ac.uk/pdbsum/6y3p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6y3p 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=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KLLA0_B12012g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284590 Candida sphaerica])</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=6y3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y3p OCA], [http://pdbe.org/6y3p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6y3p RCSB], [http://www.ebi.ac.uk/pdbsum/6y3p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6y3p ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Most eukaryotic mRNAs harbor a characteristic 5' m7GpppN cap that promotes pre-mRNA splicing, mRNA nucleocytoplasmic transport and translation while also protecting mRNAs from exonucleolytic attacks. mRNA caps are eliminated by Dcp2 during mRNA decay, allowing 5'-3' exonucleases to degrade mRNA bodies. However, the Dcp2 decapping enzyme is poorly active on its own and requires binding to stable or transient protein partners to sever the cap of target mRNAs. Here, we analyse the role of one of these partners, the yeast Pby1 factor, which is known to co-localize into P-bodies together with decapping factors. We report that Pby1 uses its C-terminal domain to directly bind to the decapping enzyme. We solved the structure of this Pby1 domain alone and bound to the Dcp1-Dcp2-Edc3 decapping complex. Structure-based mutant analyses reveal that Pby1 binding to the decapping enzyme is required for its recruitment into P-bodies. Moreover, Pby1 binding to the decapping enzyme stimulates growth in conditions in which decapping activation is compromised. Our results point towards a direct connection of Pby1 with decapping and P-body formation, both stemming from its interaction with the Dcp1-Dcp2 holoenzyme. | |||
Pby1 is a direct partner of the Dcp2 decapping enzyme.,Charenton C, Gaudon-Plesse C, Back R, Ulryck N, Cosson L, Seraphin B, Graille M Nucleic Acids Res. 2020 May 12. pii: 5836192. doi: 10.1093/nar/gkaa337. PMID:32396195<ref>PMID:32396195</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6y3p" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Candida sphaerica]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Graille M]] | [[Category: Graille, M]] | ||
[[Category: Atp-grasp]] | |||
[[Category: Ligase]] | |||
Latest revision as of 09:15, 20 May 2020
Crystal structure of the C-terminal domain from K. lactis Pby1, an ATP-grasp enzyme interacting with the mRNA decapping enzyme Dcp2Crystal structure of the C-terminal domain from K. lactis Pby1, an ATP-grasp enzyme interacting with the mRNA decapping enzyme Dcp2
Structural highlights
Publication Abstract from PubMedMost eukaryotic mRNAs harbor a characteristic 5' m7GpppN cap that promotes pre-mRNA splicing, mRNA nucleocytoplasmic transport and translation while also protecting mRNAs from exonucleolytic attacks. mRNA caps are eliminated by Dcp2 during mRNA decay, allowing 5'-3' exonucleases to degrade mRNA bodies. However, the Dcp2 decapping enzyme is poorly active on its own and requires binding to stable or transient protein partners to sever the cap of target mRNAs. Here, we analyse the role of one of these partners, the yeast Pby1 factor, which is known to co-localize into P-bodies together with decapping factors. We report that Pby1 uses its C-terminal domain to directly bind to the decapping enzyme. We solved the structure of this Pby1 domain alone and bound to the Dcp1-Dcp2-Edc3 decapping complex. Structure-based mutant analyses reveal that Pby1 binding to the decapping enzyme is required for its recruitment into P-bodies. Moreover, Pby1 binding to the decapping enzyme stimulates growth in conditions in which decapping activation is compromised. Our results point towards a direct connection of Pby1 with decapping and P-body formation, both stemming from its interaction with the Dcp1-Dcp2 holoenzyme. Pby1 is a direct partner of the Dcp2 decapping enzyme.,Charenton C, Gaudon-Plesse C, Back R, Ulryck N, Cosson L, Seraphin B, Graille M Nucleic Acids Res. 2020 May 12. pii: 5836192. doi: 10.1093/nar/gkaa337. PMID:32396195[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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