5lop

Structure of the active form of /K. lactis/ Dcp1-Dcp2-Edc3 decapping complex bound to m7GDP

spinqualitylabelsall models 5lop, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5lop is a 3 chain structure with sequence from Kluyveromyces lactis NRRL Y-1140. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.5Å Ligands: M7G, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6CPV9_KLULA 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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