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5lop
From Proteopedia
(Difference between revisions)
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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=5lop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lop OCA], [http://pdbe.org/5lop PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lop RCSB], [http://www.ebi.ac.uk/pdbsum/5lop PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lop ProSAT]</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=5lop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lop OCA], [http://pdbe.org/5lop PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lop RCSB], [http://www.ebi.ac.uk/pdbsum/5lop PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lop ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Elimination of the 5' cap of eukaryotic mRNAs, known as decapping, is considered to be a crucial, irreversible and highly regulated step required for the rapid degradation of mRNA by Xrn1, the major cytoplasmic 5'-3' exonuclease. Decapping is accomplished by the recruitment of a protein complex formed by the Dcp2 catalytic subunit and its Dcp1 cofactor. However, this complex has a low intrinsic enzymatic activity and requires several accessory proteins such as the Lsm1-7 complex, Pat1, Edc1-Edc2 and/or Edc3 to be fully active. Here we present the crystal structure of the active form of the yeast Kluyveromyces lactis Dcp1-Dcp2 enzyme bound to its product (m7GDP) and its potent activator Edc3. This structure of the Dcp1-Dcp2 complex bound to a cap analog further explains previously published data on substrate binding and provides hints as to the mechanism of Edc3-mediated Dcp2 activation. | ||
| + | |||
| + | Structure of the active form of Dcp1-Dcp2 decapping enzyme bound to m7GDP and its Edc3 activator.,Charenton C, Taverniti V, Gaudon-Plesse C, Back R, Seraphin B, Graille M Nat Struct Mol Biol. 2016 Oct 3. doi: 10.1038/nsmb.3300. PMID:27694841<ref>PMID:27694841</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5lop" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:13, 19 October 2016
Structure of the active form of /K. lactis/ Dcp1-Dcp2-Edc3 decapping complex bound to m7GDP
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