5LON

Structure of /K. lactis/ Dcp1-Dcp2 decapping complex.

Summary for 5LON

• Entry DOI: 10.2210/pdb5lon/pdb
• Descriptor: KLLA0F23980p, KLLA0E01827p (2 entities in total)
• Functional Keywords: rna decay, multiprotein complex, rna binding protein
• Biological source: Kluyveromyces lactis NRRL Y-1140 (Yeast); More
• Total number of polymer chains: 2
• Total formula weight: 54564.54

Authors

Charenton, C.,Taverniti, V.,Gaudon-Plesse, C.,Back, R.,Seraphin, B.,Graille, M. (deposition date: 2016-08-09, release date: 2016-10-05, Last modification date: 2024-01-10)

Primary citation

Charenton, C.,Taverniti, V.,Gaudon-Plesse, C.,Back, R.,Seraphin, B.,Graille, M.
Structure of the active form of Dcp1-Dcp2 decapping enzyme bound to m(7)GDP and its Edc3 activator.
Nat.Struct.Mol.Biol., 23:982-986, 2016

PubMed Abstract: 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 (mGDP) 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.

PubMed: 27694841
DOI: 10.1038/nsmb.3300

Experimental method

X-RAY DIFFRACTION (3.5 Å)