5kq1

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==Crystal structure of S. pombe Dcp1/Dcp2 in complex with H. sapiens PNRC2==
==Crystal structure of S. pombe Dcp1/Dcp2 in complex with H. sapiens PNRC2==
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<StructureSection load='5kq1' size='340' side='right' caption='[[5kq1]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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<StructureSection load='5kq1' size='340' side='right'caption='[[5kq1]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5kq1]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KQ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KQ1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5kq1]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KQ1 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kq4|5kq4]]</td></tr>
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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]] 3.002&#8491;</td></tr>
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<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=5kq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kq1 OCA], [http://pdbe.org/5kq1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kq1 RCSB], [http://www.ebi.ac.uk/pdbsum/5kq1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kq1 ProSAT]</span></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=5kq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kq1 OCA], [https://pdbe.org/5kq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kq1 RCSB], [https://www.ebi.ac.uk/pdbsum/5kq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kq1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DCP1_SCHPO DCP1_SCHPO]] Component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.<ref>PMID:15671491</ref> [[http://www.uniprot.org/uniprot/DCP2_SCHPO DCP2_SCHPO]] Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.<ref>PMID:15671491</ref> [[http://www.uniprot.org/uniprot/PNRC2_HUMAN PNRC2_HUMAN]] Involved in nonsense-mediated mRNA decay (NMD) by acting as a bridge between the mRNA decapping complex and the NMD machinery. May act by targeting the NMD machinery to the P-body and recruiting the decapping machinery to aberrant mRNAs. Required for UPF1/RENT1 localization to the P-body. Also acts as a nuclear receptor coactivator. May play a role in controlling the energy balance between energy storage and energy expenditure.<ref>PMID:11574675</ref> <ref>PMID:19150429</ref>
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[https://www.uniprot.org/uniprot/DCP1_SCHPO DCP1_SCHPO] Component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.<ref>PMID:15671491</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Removal of the 5' cap on mRNA by the decapping enzyme Dcp2 is a critical step in 5'-to-3' mRNA decay. Understanding the structural basis of Dcp2 activity has been a challenge because Dcp2 is dynamic and has weak affinity for the cap substrate. Here we present a 2.6-A-resolution crystal structure of a heterotrimer of fission yeast Dcp2, its essential activator Dcp1, and the human NMD cofactor PNRC2, in complex with a tight-binding cap analog. Cap binding is accompanied by a conformational change in Dcp2, thereby forming a composite nucleotide-binding site comprising conserved residues in the catalytic and regulatory domains. Kinetic analysis of PNRC2 revealed that a conserved short linear motif enhances both substrate affinity and the catalytic step of decapping. These findings explain why Dcp2 requires a conformational change for efficient catalysis and reveals that coactivators promote RNA binding and the catalytic step of decapping, possibly through different conformational states.
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Structural basis of mRNA-cap recognition by Dcp1-Dcp2.,Mugridge JS, Ziemniak M, Jemielity J, Gross JD Nat Struct Mol Biol. 2016 Oct 3. doi: 10.1038/nsmb.3301. PMID:27694842<ref>PMID:27694842</ref>
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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 5kq1" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Gross, J D]]
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[[Category: Homo sapiens]]
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[[Category: Jemielity, J]]
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[[Category: Large Structures]]
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[[Category: Mugridge, J S]]
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[[Category: Schizosaccharomyces pombe 972h-]]
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[[Category: Ziemniak, M]]
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[[Category: Gross JD]]
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[[Category: Decapping mrna decay nudix cap analog]]
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[[Category: Jemielity J]]
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[[Category: Hydrolase]]
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[[Category: Mugridge JS]]
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[[Category: Ziemniak M]]

Current revision

Crystal structure of S. pombe Dcp1/Dcp2 in complex with H. sapiens PNRC2

PDB ID 5kq1

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