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| | <StructureSection load='4d0k' size='340' side='right'caption='[[4d0k]], [[Resolution|resolution]] 1.89Å' scene=''> | | <StructureSection load='4d0k' size='340' side='right'caption='[[4d0k]], [[Resolution|resolution]] 1.89Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4d0k]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_144.50 Cbs 144.50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D0K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D0K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4d0k]] is a 3 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=4D0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D0K FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4czv|4czv]], [[4czw|4czw]], [[4czx|4czx]], [[4czy|4czy]]</td></tr> | + | </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=4d0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d0k OCA], [https://pdbe.org/4d0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d0k RCSB], [https://www.ebi.ac.uk/pdbsum/4d0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d0k ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Poly(A)-specific_ribonuclease Poly(A)-specific ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.13.4 3.1.13.4] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d0k OCA], [http://pdbe.org/4d0k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d0k RCSB], [http://www.ebi.ac.uk/pdbsum/4d0k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d0k ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/PAN2_CHATD PAN2_CHATD]] Catalytic 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.[HAMAP-Rule:MF_03182]<ref>PMID:24872509</ref> |
| | <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: Cbs 144 50]] | + | [[Category: Chaetomium thermophilum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Izaurralde, E]] | + | [[Category: Izaurralde E]] |
| - | [[Category: Jonas, S]] | + | [[Category: Jonas S]] |
| - | [[Category: Weichenrieder, O]] | + | [[Category: Weichenrieder O]] |
| - | [[Category: C-terminal knob domain]]
| + | |
| - | [[Category: Deadenylation]]
| + | |
| - | [[Category: Gene regulation]]
| + | |
| - | [[Category: Mrna decay]]
| + | |
| - | [[Category: Pan2-pan3 complex]]
| + | |
| - | [[Category: Wd40 domain]]
| + | |
| Structural highlights
Function
[PAN2_CHATD] Catalytic 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.[HAMAP-Rule:MF_03182][1]
Publication Abstract from PubMed
The PAN2-PAN3 complex functions in general and microRNA-mediated mRNA deadenylation. However, mechanistic insight into PAN2 and its complex with the asymmetric PAN3 dimer is lacking. Here, we describe crystal structures that show that Neurospora crassa PAN2 comprises two independent structural units: a C-terminal catalytic unit and an N-terminal assembly unit that engages in a bipartite interaction with PAN3 dimers. The catalytic unit contains the exonuclease domain in an intimate complex with a potentially modulatory ubiquitin-protease-like domain. The assembly unit contains a WD40 propeller connected to an adaptable linker. The propeller contacts the PAN3 C-terminal domain, whereas the linker reinforces the asymmetry of the PAN3 dimer and prevents the recruitment of a second PAN2 molecule. Functional data indicate an essential role for PAN3 in coordinating PAN2-mediated deadenylation with subsequent steps in mRNA decay, which lead to complete mRNA degradation.
An asymmetric PAN3 dimer recruits a single PAN2 exonuclease to mediate mRNA deadenylation and decay.,Jonas S, Christie M, Peter D, Bhandari D, Loh B, Huntzinger E, Weichenrieder O, Izaurralde E Nat Struct Mol Biol. 2014 Jun 1. doi: 10.1038/nsmb.2837. PMID:24880343[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wolf J, Valkov E, Allen MD, Meineke B, Gordiyenko Y, McLaughlin SH, Olsen TM, Robinson CV, Bycroft M, Stewart M, Passmore LA. Structural basis for Pan3 binding to Pan2 and its function in mRNA recruitment and deadenylation. EMBO J. 2014 May 28. pii: e201488373. PMID:24872509 doi:http://dx.doi.org/10.15252/embj.201488373
- ↑ Jonas S, Christie M, Peter D, Bhandari D, Loh B, Huntzinger E, Weichenrieder O, Izaurralde E. An asymmetric PAN3 dimer recruits a single PAN2 exonuclease to mediate mRNA deadenylation and decay. Nat Struct Mol Biol. 2014 Jun 1. doi: 10.1038/nsmb.2837. PMID:24880343 doi:http://dx.doi.org/10.1038/nsmb.2837
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