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4q8h

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(New page: '''Unreleased structure''' The entry 4q8h is ON HOLD Authors: Schaefer, I.B., Conti, E. Description: Structure of the Saccharomyces cerevisiae PAN2 pseudoubiquitin-hydrolase-RNase modu...)
Current revision (17:29, 20 September 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 4q8h is ON HOLD
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==Structure of the Saccharomyces cerevisiae PAN2 pseudoubiquitin-hydrolase-RNase module==
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<StructureSection load='4q8h' size='340' side='right'caption='[[4q8h]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4q8h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q8H FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4q8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q8h OCA], [https://pdbe.org/4q8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q8h RCSB], [https://www.ebi.ac.uk/pdbsum/4q8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q8h ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PAN2_YEAST PAN2_YEAST] 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 when the poly(A) stretch is bound by poly(A)-binding protein PAB1, which 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 by DCP1-DCP2 and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails, trimming the tails from their synthesized length to the slightly shorter, apparently messenger-specific length found on newly exported mRNAs. PAN cooperates with protein kinase DUN1 in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress.<ref>PMID:8550599</ref> <ref>PMID:1358757</ref> <ref>PMID:8816488</ref> <ref>PMID:9774670</ref> <ref>PMID:11239395</ref> <ref>PMID:11953437</ref> <ref>PMID:15630021</ref> <ref>PMID:15894541</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Pan2-Pan3 is a conserved complex involved in the shortening of mRNA poly(A) tails, the initial step in eukaryotic mRNA turnover. We show that recombinant Saccharomyces cerevisiae Pan2-Pan3 can deadenylate RNAs in vitro without needing the poly(A)-binding protein Pab1. The crystal structure of an active ~200-kDa core complex reveals that Pan2 and Pan3 interact with an unusual 1:2 stoichiometry imparted by the asymmetric nature of the Pan3 homodimer. An extended region of Pan2 wraps around Pan3 and provides a major anchoring point for complex assembly. A Pan2 module formed by the pseudoubiquitin-hydrolase and RNase domains latches onto the Pan3 pseudokinase with intertwined interactions that orient the deadenylase active site toward the A-binding site of the interacting Pan3. The molecular architecture of Pan2-Pan3 suggests how the nuclease and its pseudokinase regulator act in synergy to promote deadenylation.
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Authors: Schaefer, I.B., Conti, E.
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The structure of the Pan2-Pan3 core complex reveals cross-talk between deadenylase and pseudokinase.,Schafer IB, Rode M, Bonneau F, Schussler S, Conti E Nat Struct Mol Biol. 2014 Jun 1. doi: 10.1038/nsmb.2834. PMID:24880344<ref>PMID:24880344</ref>
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Description: Structure of the Saccharomyces cerevisiae PAN2 pseudoubiquitin-hydrolase-RNase module
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4q8h" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Conti E]]
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[[Category: Schaefer IB]]

Current revision

Structure of the Saccharomyces cerevisiae PAN2 pseudoubiquitin-hydrolase-RNase module

PDB ID 4q8h

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