3rv1

Crystal structure of the N-terminal and RNase III domains of K. polysporus Dcr1 E224Q mutant

spinqualitylabelsall models 3rv1, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3rv1 is a 2 chain structure with sequence from Kluyveromyces polysporus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3rv0 Gene: Kpol_455p11 (Kluyveromyces polysporus) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The Dicer ribonuclease III (RNase III) enzymes process long double-stranded RNA (dsRNA) into small interfering RNAs (siRNAs) that direct RNA interference. Here, we describe the structure and activity of a catalytically active fragment of Kluyveromyces polysporus Dcr1, which represents the noncanonical Dicers found in budding yeasts. The crystal structure revealed a homodimer resembling that of bacterial RNase III but extended by a unique N-terminal domain, and it identified additional catalytic residues conserved throughout eukaryotic RNase III enzymes. Biochemical analyses showed that Dcr1 dimers bind cooperatively along the dsRNA substrate such that the distance between consecutive active sites determines the length of the siRNA products. Thus, unlike canonical Dicers, which successively remove siRNA duplexes from the dsRNA termini, budding-yeast Dicers initiate processing in the interior and work outward. The distinct mechanism of budding-yeast Dicers establishes a paradigm for natural molecular rulers and imparts substrate preferences with ramifications for biological function. The inside-out mechanism of dicers from budding yeasts.,Weinberg DE, Nakanishi K, Patel DJ, Bartel DP Cell. 2011 Jul 22;146(2):262-76. PMID:21784247 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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