4q2s | pdb_00004q2s

Crystal Structure of S. pombe Pdc1 Ge1 Domain

spinqualitylabelsall models 4q2s, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4q2s is a 1 chain structure with sequence from Schizosaccharomyces pombe 972h-. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function YE38_SCHPO Publication Abstract from PubMed In eukaryotic cells, components of the 5' to 3' mRNA degradation machinery can undergo a rapid phase transition. The resulting cytoplasmic foci are referred to as processing bodies (P-bodies). The molecular details of the self-aggregation process are, however, largely undetermined. Herein, we use a bottom-up approach that combines NMR spectroscopy, isothermal titration calorimetry, X-ray crystallography, and fluorescence microscopy to probe if mRNA degradation factors can undergo phase transitions in vitro. We show that the Schizosaccharomyces pombe Dcp2 mRNA decapping enzyme, its prime activator Dcp1, and the scaffolding proteins Edc3 and Pdc1 are sufficient to reconstitute a phase-separation process. Intermolecular interactions between the Edc3 LSm domain and at least 10 helical leucine-rich motifs in Dcp2 and Pdc1 build the core of the interaction network. We show that blocking of these interactions interferes with the clustering behavior, both in vitro and in vivo. In vitro reconstitution of a cellular phase-transition process that involves the mRNA decapping machinery.,Fromm SA, Kamenz J, Noldeke ER, Neu A, Zocher G, Sprangers R Angew Chem Int Ed Engl. 2014 Jul 7;53(28):7354-9. doi: 10.1002/anie.201402885., Epub 2014 May 26. PMID:24862735 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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