2qkm | pdb_00002qkm

The crystal structure of fission yeast mRNA decapping enzyme Dcp1-Dcp2 complex

spinqualitylabelsall models 2qkm, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2qkm is a 8 chain structure with sequence from Schizosaccharomyces pombe. The January 2012 RCSB PDB Molecule of the Month feature on Messenger RNA Capping by David Goodsell is 10.2210/rcsb_pdb/mom_2012_1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP Related: 2qkl, 2a6t Gene: dcp1 (Schizosaccharomyces pombe), SPAC19A8.12 (Schizosaccharomyces pombe) Activity: M(7)G(5')pppN diphosphatase, with EC number 3.6.1.30 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed A critical step in mRNA degradation is the removal of the 5' cap structure, which is catalyzed by the Dcp1-Dcp2 complex. The crystal structure of an S. pombe Dcp1p-Dcp2n complex combined with small-angle X-ray scattering analysis (SAXS) reveals that Dcp2p exists in open and closed conformations, with the closed complex being, or closely resembling, the catalytically more active form. This suggests that a conformational change between these open and closed complexes might control decapping. A bipartite RNA-binding channel containing the catalytic site and Box B motif is identified with a bound ATP located in the catalytic pocket in the closed complex, suggesting possible interactions that facilitate substrate binding. Dcp1 stimulates the activity of Dcp2 by promoting and/or stabilizing the closed complex. Notably, the interface of Dcp1 and Dcp2 is not fully conserved, explaining why the Dcp1-Dcp2 interaction in higher eukaryotes requires an additional factor. Structural basis of dcp2 recognition and activation by dcp1.,She M, Decker CJ, Svergun DI, Round A, Chen N, Muhlrad D, Parker R, Song H Mol Cell. 2008 Feb 15;29(3):337-49. PMID:18280239 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA