4cyi
From Proteopedia
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==Chaetomium thermophilum Pan3== | ==Chaetomium thermophilum Pan3== | ||
- | <StructureSection load='4cyi' size='340' side='right' caption='[[4cyi]], [[Resolution|resolution]] 2.42Å' scene=''> | + | <StructureSection load='4cyi' size='340' side='right'caption='[[4cyi]], [[Resolution|resolution]] 2.42Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[4cyi]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CYI OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[4cyi]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CYI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CYI FirstGlance]. <br> |
- | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=4cyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cyi OCA], [https://pdbe.org/4cyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cyi RCSB], [https://www.ebi.ac.uk/pdbsum/4cyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cyi ProSAT]</span></td></tr> | |
- | <tr | + | </table> |
- | + | == Function == | |
- | <table> | + | [[https://www.uniprot.org/uniprot/PAN3_CHATD PAN3_CHATD]] Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and with PAB1.[HAMAP-Rule:MF_03181]<ref>PMID:24872509</ref> |
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The conserved eukaryotic Pan2-Pan3 deadenylation complex shortens cytoplasmic mRNA 3' polyA tails to regulate mRNA stability. Although the exonuclease activity resides in Pan2, efficient deadenylation requires Pan3. The mechanistic role of Pan3 is unclear. Here, we show that Pan3 binds RNA directly both through its pseudokinase/C-terminal domain and via an N-terminal zinc finger that binds polyA RNA specifically. In contrast, isolated Pan2 is unable to bind RNA. Pan3 binds to the region of Pan2 that links its N-terminal WD40 domain to the C-terminal part that contains the exonuclease, with a 2:1 stoichiometry. The crystal structure of the Pan2 linker region bound to a Pan3 homodimer shows how the unusual structural asymmetry of the Pan3 dimer is used to form an extensive high-affinity interaction. This binding allows Pan3 to supply Pan2 with substrate polyA RNA, facilitating efficient mRNA deadenylation by the intact Pan2-Pan3 complex. | ||
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+ | Structural basis for Pan3 binding to Pan2 and its function in mRNA recruitment and deadenylation.,Wolf J, Valkov E, Allen MD, Meineke B, Gordiyenko Y, McLaughlin SH, Olsen TM, Robinson CV, Bycroft M, Stewart M, Passmore LA EMBO J. 2014 May 28. pii: e201488373. PMID:24872509<ref>PMID:24872509</ref> | ||
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+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 4cyi" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Allen | + | [[Category: Chaetomium thermophilum]] |
- | [[Category: Bycroft | + | [[Category: Large Structures]] |
- | [[Category: Gordiyenko | + | [[Category: Allen MD]] |
- | [[Category: McLaughlin | + | [[Category: Bycroft M]] |
- | [[Category: Meineke | + | [[Category: Gordiyenko Y]] |
- | [[Category: Olsen | + | [[Category: McLaughlin SH]] |
- | [[Category: Passmore | + | [[Category: Meineke B]] |
- | [[Category: Robinson | + | [[Category: Olsen TM]] |
- | [[Category: Stewart | + | [[Category: Passmore LA]] |
- | [[Category: Valkov | + | [[Category: Robinson CV]] |
- | [[Category: Wolf | + | [[Category: Stewart M]] |
- | + | [[Category: Valkov E]] | |
+ | [[Category: Wolf J]] |
Current revision
Chaetomium thermophilum Pan3
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